Proteopedia - User contributions [en]

https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Garrett+Leibow Proteopedia - User contributions [en] 2026-10-06T20:10:25Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122960 Sandbox Reserved 1563 2019-12-09T05:55:20Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less frequently and thus uncontrolled cell division would become less likely. Dinucleoside polyphosphates used as IMPDH inhibitors may contribute as anticancer and antiviral drugs<ref>PMID: 21517780</ref>.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> In the <scene name='82/823087/Impdh_secondary_structures/4'>IMPDH secondary structures</scene>. Alpha and beta sheets are shown. The active site of the protein is located on the C-terminus end in the TIM barrel. This contains 8 beta sheets and 8 alpha helices.<br /> <br /> <scene name='82/823087/Impdh_quat_structure/1'>IMPDH quaternary structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of <scene name='82/823087/Impdh_tertiary_structure/1'>tertiary structures</scene>. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> The <scene name='82/823087/Impdh_space_fill/1'>IMPDH space filled</scene> is important to get a more accurate representation of the amount of space the protein would take up. It better shows the interactions in the structure. In the image the light blue is the amino acid residues. The red dots represent water molecules. The orange is phosphorus. Lastly the blue is nitrogen.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/4'>IMPDH hydrophobicity view</scene>. The hydrophilic residues interact with the outside enviornment. They contain amino acid residues that can hydrogen bond and are used to maintain structure for the active binding site. The hydrophobic region (Gly 361 and Gly 383) interacts with the phosphate chain. This will allow for more movement of the cations.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/5'>IMPDH ligand view</scene>. Ligands for this structure include GDP and G5P ions. The ligands of NAD, G5P, and GDP will form hydrogen and hydrophobic bonds between each other. When cations pass through they will interact with the phosphates.<br /> <br /> <scene name='82/823087/Impdh_triad/6'>IMPDH triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid black structures in the image. This triad is important as it makes cysteine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/5'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cysteine more reactive and binding is induced. In the image the cysteines are in white. This is where binding would occur. So for this image the cysteines that are made more reactive are shown in light green. Asp 259 (shown in red in this image) hydrogen bonds to ribose hydroxyls and Ser 315 (also shown in red) hydrogen bonds to ribose phosphate. Gly 383 (Shown in Light blue) interacts with NAD through hydrophobic interactions. Gly 361 (also light blue) binds to NAD through hydrophobic interactions as well.<br /> <br /> <scene name='82/823087/Impdh_charge/2'>IMPDH charge</scene>. IMPDH has no significant charge since it is found in physiological environments. Positively and negatively charged amino acids play a part in intermediate covalent binding steps<ref>PMID: 31416831</ref>. <br /> <br /> <scene name='82/823087/Impdh_composition/2'>IMPDH composition</scene>. G5P and GDP ligands are shown in Pink. The green represents the anions that, during the intermediate step, function as ligands. Cations will travel through an active IMPDH.<br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the Bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates, and the affinity for those binding sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with purine mononucleotides within the Bateman domain. This requires the Bateman domain to make IMPDH more sensitive to inhibition<ref>PMID: 10390600</ref>. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122957 Sandbox Reserved 1563 2019-12-09T05:51:15Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less frequently and thus uncontrolled cell division would become less likely. Dinucleoside polyphosphates used as IMPDH inhibitors may contribute as anticancer and antiviral drugs<ref>PMID: 21517780</ref>.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> In the <scene name='82/823087/Impdh_secondary_structures/4'>IMPDH secondary structures</scene>. Alpha and beta sheets are shown. The active site of the protein is located on the C-terminus end in the TIM barrel. This contains 8 beta sheets and 8 alpha helices.<br /> <br /> <scene name='82/823087/Impdh_quat_structure/1'>IMPDH quaternary structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of <scene name='82/823087/Impdh_tertiary_structure/1'>tertiary structures</scene>. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> The <scene name='82/823087/Impdh_space_fill/1'>IMPDH space filled</scene> is important to get a more accurate representation of the amount of space the protein would take up. It better shows the interactions in the structure. In the image the light blue is the amino acid residues. The red dots represent water molecules. The orange is phosphorus. Lastly the blue is nitrogen.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/4'>IMPDH hydrophobicity view</scene>. The hydrophilic residues interact with the outside enviornment. They contain amino acid residues that can hydrogen bond and are used to maintain structure for the active binding site. The hydrophobic region (Gly 361 and Gly 383) interacts with the phosphate chain. This will allow for more movement of the cations.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/5'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/6'>IMPDH triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid black structures in the image. This triad is important as it makes cysteine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/5'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cysteine more reactive and binding is induced. In the image the cysteines are in white. This is where binding would occur. So for this image the cysteines that are made more reactive are shown in light green. Asp 259 (shown in red in this image) hydrogen bonds to ribose hydroxyls and Ser 315 (also shown in red) hydrogen bonds to ribose phosphate. Gly 383 (Shown in Light blue) interacts with NAD through hydrophobic interactions. Gly 361 (also light blue) binds to NAD through hydrophobic interactions as well.<br /> <br /> <scene name='82/823087/Impdh_charge/2'>IMPDH charge</scene>. IMPDH has no significant charge since it is found in physiological environments. Positively and negatively charged amino acids play a part in intermediate covalent binding steps<ref>PMID: 31416831</ref>. <br /> <br /> <scene name='82/823087/Impdh_composition/2'>IMPDH composition</scene>. G5P and GDP ligands are shown in Pink. The green represents the anions that, during the intermediate step, function as ligands. Cations will travel through an active IMPDH.<br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the Bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates, and the affinity for those binding sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with purine mononucleotides within the Bateman domain. This requires the Bateman domain to make IMPDH more sensitive to inhibition<ref>PMID: 10390600</ref>. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122949 Sandbox Reserved 1563 2019-12-09T05:41:00Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less frequently and thus uncontrolled cell division would become less likely. Dinucleoside polyphosphates used as IMPDH inhibitors may contribute as anticancer and antiviral drugs<ref>PMID: 21517780</ref>.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> In the <scene name='82/823087/Impdh_secondary_structures/4'>IMPDH secondary structures</scene>. Alpha and beta sheets are shown. The active site of the protein is located on the C-terminus end in the TIM barrel. This contains 8 beta sheets and 8 alpha helices.<br /> <br /> <scene name='82/823087/Impdh_quat_structure/1'>IMPDH quaternary structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of <scene name='82/823087/Impdh_tertiary_structure/1'>tertiary structures</scene>. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> The <scene name='82/823087/Impdh_space_fill/1'>IMPDH space filled</scene> is important to get a more accurate representation of the amount of space the protein would take up. It better shows the interactions in the structure. In the image the light blue is the amino acid residues. The red dots represent water molecules. The orange is phosphorus. Lastly the blue is nitrogen.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/4'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/5'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/6'>IMPDH triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid black structures in the image. This triad is important as it makes cysteine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/5'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cysteine more reactive and binding is induced. In the image the cysteines are in white. This is where binding would occur. So for this image the cysteines that are made more reactive are shown in light green. Asp 259 (shown in red in this image) hydrogen bonds to ribose hydroxyls and Ser 315 (also shown in red) hydrogen bonds to ribose phosphate. Gly 383 (Shown in Light blue) interacts with NAD through hydrophobic interactions. Gly 361 (also light blue) binds to NAD through hydrophobic interactions as well.<br /> <br /> <scene name='82/823087/Impdh_charge/2'>IMPDH charge</scene>. IMPDH has no significant charge since it is found in physiological environments. Positively and negatively charged amino acids play a part in intermediate covalent binding steps<ref>PMID: 31416831</ref>. <br /> <br /> <scene name='82/823087/Impdh_composition/2'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the Bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates, and the affinity for those binding sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with purine mononucleotides within the Bateman domain. This requires the Bateman domain to make IMPDH more sensitive to inhibition<ref>PMID: 10390600</ref>. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122931 Sandbox Reserved 1563 2019-12-09T05:24:01Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less frequently and thus uncontrolled cell division would become less likely. Dinucleoside polyphosphates used as IMPDH inhibitors may contribute as anticancer and antiviral drugs<ref>PMID: 21517780</ref>.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> In the <scene name='82/823087/Impdh_secondary_structures/4'>IMPDH secondary structures</scene>. Alpha and beta sheets are shown. The active site of the protein is located on the C-terminus end in the TIM barrel. This contains 8 beta sheets and 8 alpha helices.<br /> <br /> <scene name='82/823087/Impdh_quat_structure/1'>IMPDH quaternary structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of <scene name='82/823087/Impdh_tertiary_structure/1'>tertiary structures</scene>. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_space_fill/1'>IMPDH space filled</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/4'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/5'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/6'>IMPDH triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid black structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/5'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/2'>IMPDH charge</scene>. IMPDH has no significant charge since it is found in physiological environments. Positively and negatively charged amino acids play a part in intermediate covalent binding steps<ref>PMID: 31416831</ref>. <br /> <br /> <scene name='82/823087/Impdh_composition/2'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the Bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates, and the affinity for those binding sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with purine mononucleotides within the Bateman domain. This requires the Bateman domain to make IMPDH more sensitive to inhibition<ref>PMID: 10390600</ref>. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122926 Sandbox Reserved 1563 2019-12-09T05:13:54Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less frequently and thus uncontrolled cell division would become less likely. Dinucleoside polyphosphates used as IMPDH inhibitors may contribute as anticancer and antiviral drugs<ref>PMID: 21517780</ref>.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structures/4'>IMPDH secondary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_quat_structure/1'>IMPDH quaternary structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_tertiary_structure/1'>IMPDH Tertiary strucure</scene>.<br /> <br /> <scene name='82/823087/Impdh_space_fill/1'>IMPDH space filled</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/4'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/5'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/6'>IMPDH triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid black structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/5'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/2'>IMPDH charge</scene>. IMPDH has no significant charge since it is found in physiological environments. Positively and negatively charged amino acids play a part in intermediate covalent binding steps<ref>PMID: 31416831</ref>. <br /> <br /> <scene name='82/823087/Impdh_composition/2'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the Bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates, and the affinity for those binding sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with purine mononucleotides within the Bateman domain. This requires the Bateman domain to make IMPDH more sensitive to inhibition<ref>PMID: 10390600</ref>. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122913 Sandbox Reserved 1563 2019-12-09T04:45:10Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less frequently and thus uncontrolled cell division would become less likely. Dinucleoside polyphosphates used as IMPDH inhibitors may contribute as anticancer and antiviral drugs<ref>PMID: 21517780</ref>.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structures/4'>IMPDH secondary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_quat_structure/1'>IMPDH quaternary structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> IMPDH Tertiary strucure.<br /> <br /> <scene name='82/823087/Impdh_space_fill/1'>IMPDH space filled</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/4'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/5'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/6'>IMPDH triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid black structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/5'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/2'>IMPDH charge</scene>. IMPDH has no significant charge since it is found in physiological environments. Positively and negatively charged amino acids play a part in intermediate covalent binding steps<ref>PMID: 31416831</ref>. <br /> <br /> <scene name='82/823087/Impdh_composition/2'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the Bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates, and the affinity for those binding sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with purine mononucleotides within the Bateman domain. This requires the Bateman domain to make IMPDH more sensitive to inhibition<ref>PMID: 10390600</ref>. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122907 Sandbox Reserved 1563 2019-12-09T04:26:37Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less frequently and thus uncontrolled cell division would become less likely. Dinucleoside polyphosphates used as IMPDH inhibitors may contribute as anticancer and antiviral drugs<ref>PMID: 21517780</ref>.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structures/4'>IMPDH secondary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/2'>IMPDH quaternary structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_space_fill/1'>IMPDH space filled</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/4'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/5'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/6'>IMPDH triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid black structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/5'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/2'>IMPDH charge</scene>. IMPDH has no significant charge since it is found in physiological environments. Positively and negatively charged amino acids play a part in intermediate covalent binding steps<ref>PMID: 31416831</ref>. <br /> <br /> <scene name='82/823087/Impdh_composition/2'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the Bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates, and the affinity for those binding sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with purine mononucleotides within the Bateman domain. This requires the Bateman domain to make IMPDH more sensitive to inhibition<ref>PMID: 10390600</ref>. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122897 Sandbox Reserved 1563 2019-12-09T03:28:07Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less frequently and thus uncontrolled cell division would become less likely. Dinucleoside polyphosphates used as IMPDH inhibitors may contribute as anticancer and antiviral drugs<ref>PMID: 21517780</ref>.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structures/4'>IMPDH secondary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/2'>IMPDH quaternary structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_space_fill/1'>IMPDH space filled</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/4'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/5'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/6'>IMPDH triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid black structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/4'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/2'>IMPDH charge</scene>. IMPDH has no significant charge since it is found in physiological environments. Positively and negatively charged amino acids play a part in intermediate covalent binding steps<ref>PMID: 31416831</ref>. <br /> <br /> <scene name='82/823087/Impdh_composition/2'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the Bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates, and the affinity for those binding sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with purine mononucleotides within the Bateman domain. This requires the Bateman domain to make IMPDH more sensitive to inhibition<ref>PMID: 10390600</ref>. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122894 Sandbox Reserved 1563 2019-12-09T03:12:48Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less frequently and thus uncontrolled cell division would become less likely. Dinucleoside polyphosphates used as IMPDH inhibitors may contribute as anticancer and antiviral drugs<ref>PMID: 21517780</ref>.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structures/4'>IMPDH secondary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/2'>IMPDH quaternary structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_space_fill/1'>IMPDH space filled</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/4'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/5'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/6'>IMPDH triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid black structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/2'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/2'>IMPDH charge</scene>. IMPDH has no significant charge since it is found in physiological environments. Positively and negatively charged amino acids play a part in intermediate covalent binding steps<ref>PMID: 31416831</ref>. <br /> <br /> <scene name='82/823087/Impdh_composition/2'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the Bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates, and the affinity for those binding sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with purine mononucleotides within the Bateman domain. This requires the Bateman domain to make IMPDH more sensitive to inhibition<ref>PMID: 10390600</ref>. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122873 Sandbox Reserved 1563 2019-12-09T02:41:17Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less frequently and thus uncontrolled cell division would become less likely. Dinucleoside polyphosphates used as IMPDH inhibitors may contribute as anticancer and antiviral drugs<ref>PMID: 21517780</ref>.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structures/4'>IMPDH secondary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/2'>IMPDH quaternary structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_space_fill/1'>IMPDH space filled</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/4'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/5'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/5'>IMPDH triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid black structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/2'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/2'>IMPDH charge</scene>. IMPDH has no significant charge since it is found in physiological environments. Positively and negatively charged amino acids play a part in intermediate covalent binding steps<ref>PMID: 31416831</ref>. <br /> <br /> <scene name='82/823087/Impdh_composition/2'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the Bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates, and the affinity for those binding sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with purine mononucleotides within the Bateman domain. This requires the Bateman domain to make IMPDH more sensitive to inhibition<ref>PMID: 10390600</ref>. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122870 Sandbox Reserved 1563 2019-12-09T02:38:44Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less frequently and thus uncontrolled cell division would become less likely. Dinucleoside polyphosphates used as IMPDH inhibitors may contribute as anticancer and antiviral drugs<ref>PMID: 21517780</ref>.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structures/4'>IMPDH secondary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/2'>IMPDH quaternary structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_space_fill/1'>IMPDH space filled</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/4'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/4'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/5'>IMPDH triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid black structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/2'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/2'>IMPDH charge</scene>. IMPDH has no significant charge since it is found in physiological environments. Positively and negatively charged amino acids play a part in intermediate covalent binding steps<ref>PMID: 31416831</ref>. <br /> <br /> <scene name='82/823087/Impdh_composition/2'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the Bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates, and the affinity for those binding sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with purine mononucleotides within the Bateman domain. This requires the Bateman domain to make IMPDH more sensitive to inhibition<ref>PMID: 10390600</ref>. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122726 Sandbox Reserved 1563 2019-12-08T19:30:46Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less frequently and thus uncontrolled cell division would become less likely. Dinucleoside polyphosphates used as IMPDH inhibitors may contribute as anticancer and antiviral drugs<ref>PMID: 21517780</ref>.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structures/4'>IMPDH secondary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/2'>IMPDH quaternary structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_space_fill/1'>IMPDH space filled</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/4'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/3'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/5'>IMPDH triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid black structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/2'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/2'>IMPDH charge</scene>. IMPDH has no significant charge since it is found in physiological environments. Positively and negatively charged amino acids play a part in intermediate covalent binding steps<ref>PMID: 31416831</ref>. <br /> <br /> <scene name='82/823087/Impdh_composition/2'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the Bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates, and the affinity for those binding sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with purine mononucleotides within the Bateman domain. This requires the Bateman domain to make IMPDH more sensitive to inhibition<ref>PMID: 10390600</ref>. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122725 Sandbox Reserved 1563 2019-12-08T19:27:28Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less frequently and thus uncontrolled cell division would become less likely. Dinucleoside polyphosphates used as IMPDH inhibitors may contribute as anticancer and antiviral drugs<ref>PMID: 21517780</ref>.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structures/4'>IMPDH secondary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/2'>IMPDH quaternary structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_space_fill/1'>IMPDH space filled</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/4'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/3'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/5'>IMPDH triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid black structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/2'>IMPDH charge</scene>. IMPDH has no significant charge since it is found in physiological environments. Positively and negatively charged amino acids play a part in intermediate covalent binding steps<ref>PMID: 31416831</ref>. <br /> <br /> <scene name='82/823087/Impdh_composition/2'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the Bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates, and the affinity for those binding sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with purine mononucleotides within the Bateman domain. This requires the Bateman domain to make IMPDH more sensitive to inhibition<ref>PMID: 10390600</ref>. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122722 Sandbox Reserved 1563 2019-12-08T18:58:16Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less frequently and thus uncontrolled cell division would become less likely. Dinucleoside polyphosphates used as IMPDH inhibitors may contribute as anticancer and antiviral drugs<ref>PMID: 21517780</ref>.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structures/4'>IMPDH secondary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/2'>IMPDH quaternary structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_space_fill/1'>IMPDH space filled</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/4'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/3'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/5'>IMPDH triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid black structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge since it is found in physiological environments. Positively and negatively charged amino acids play a part in intermediate covalent binding steps<ref>PMID: 31416831</ref>. <br /> <br /> <scene name='82/823087/Impdh_composition/2'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the Bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates, and the affinity for those binding sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with purine mononucleotides within the Bateman domain. This requires the Bateman domain to make IMPDH more sensitive to inhibition<ref>PMID: 10390600</ref>. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122719 Sandbox Reserved 1563 2019-12-08T18:34:20Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less frequently and thus uncontrolled cell division would become less likely. Dinucleoside polyphosphates used as IMPDH inhibitors may contribute as anticancer and antiviral drugs<ref>PMID: 21517780</ref>.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structures/4'>IMPDH secondary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/2'>IMPDH quaternary structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_space_fill/1'>IMPDH space filled</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/4'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/3'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/5'>IMPDH triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid black structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge since it is found in physiological environments. Positively and negatively charged amino acids play a part in intermediate covalent binding steps<ref>PMID: 31416831</ref>. <br /> <br /> <scene name='82/823087/Impdh_composition/1'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the Bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates, and the affinity for those binding sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with purine mononucleotides within the Bateman domain. This requires the Bateman domain to make IMPDH more sensitive to inhibition<ref>PMID: 10390600</ref>. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122717 Sandbox Reserved 1563 2019-12-08T18:12:24Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less frequently and thus uncontrolled cell division would become less likely. Dinucleoside polyphosphates used as IMPDH inhibitors may contribute as anticancer and antiviral drugs<ref>PMID: 21517780</ref>.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structures/4'>IMPDH secondary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/2'>IMPDH quaternary structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_space_fill/1'>IMPDH space filled</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/4'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/3'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid red structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge since it is found in physiological environments. Positively and negatively charged amino acids play a part in intermediate covalent binding steps<ref>PMID: 31416831</ref>. <br /> <br /> <scene name='82/823087/Impdh_composition/1'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the Bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates, and the affinity for those binding sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with purine mononucleotides within the Bateman domain. This requires the Bateman domain to make IMPDH more sensitive to inhibition<ref>PMID: 10390600</ref>. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122716 Sandbox Reserved 1563 2019-12-08T18:06:15Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less frequently and thus uncontrolled cell division would become less likely. Dinucleoside polyphosphates used as IMPDH inhibitors may contribute as anticancer and antiviral drugs<ref>PMID: 21517780</ref>.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structures/4'>IMPDH secondary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/2'>IMPDH quaternary structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_space_fill/1'>IMPDH space filled</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/4'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/2'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid red structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge since it is found in physiological environments. Positively and negatively charged amino acids play a part in intermediate covalent binding steps<ref>PMID: 31416831</ref>. <br /> <br /> <scene name='82/823087/Impdh_composition/1'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the Bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates, and the affinity for those binding sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with purine mononucleotides within the Bateman domain. This requires the Bateman domain to make IMPDH more sensitive to inhibition<ref>PMID: 10390600</ref>. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122713 Sandbox Reserved 1563 2019-12-08T17:38:17Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less frequently and thus uncontrolled cell division would become less likely. Dinucleoside polyphosphates used as IMPDH inhibitors may contribute as anticancer and antiviral drugs<ref>PMID: 21517780</ref>.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structures/4'>IMPDH secondary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/2'>IMPDH quaternary structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_space_fill/1'>IMPDH space filled</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/2'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid red structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge since it is found in physiological environments. Positively and negatively charged amino acids play a part in intermediate covalent binding steps<ref>PMID: 31416831</ref>. <br /> <br /> <scene name='82/823087/Impdh_composition/1'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the Bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates, and the affinity for those binding sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with purine mononucleotides within the Bateman domain. This requires the Bateman domain to make IMPDH more sensitive to inhibition<ref>PMID: 10390600</ref>. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122712 Sandbox Reserved 1563 2019-12-08T17:37:14Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less frequently and thus uncontrolled cell division would become less likely. Dinucleoside polyphosphates used as IMPDH inhibitors may contribute as anticancer and antiviral drugs<ref>PMID: 21517780</ref>.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structures/4'>IMPDH secondary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/2'>IMPDH quaternary structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_space_fill/1'>IMPDH space filled</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/2'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid red structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge since it is found in physiological environments. Positively and negatively charged amino acids play a part in intermediate covalent binding steps<ref>PMID: 31416831</ref>. <br /> <br /> <scene name='82/823087/Impdh_composition/1'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the Bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates, and the affinity for those binding sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with purine mononucleotides within the Bateman domain. This requires the Bateman domain to make IMPDH more sensitive to inhibition<ref>PMID: 10390600</ref>. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122711 Sandbox Reserved 1563 2019-12-08T17:31:39Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less frequently and thus uncontrolled cell division would become less likely. Dinucleoside polyphosphates used as IMPDH inhibitors may contribute as anticancer and antiviral drugs<ref>PMID: 21517780</ref>.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structures/2'>IMPDH secondary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/2'>IMPDH_quaternary_structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_space_fill/1'>IMPDH_space_filled</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/2'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid red structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge since it is found in physiological environments. Positively and negatively charged amino acids play a part in intermediate covalent binding steps<ref>PMID: 31416831</ref>. <br /> <br /> <scene name='82/823087/Impdh_composition/1'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the Bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates, and the affinity for those binding sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with purine mononucleotides within the Bateman domain. This requires the Bateman domain to make IMPDH more sensitive to inhibition<ref>PMID: 10390600</ref>. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122635 Sandbox Reserved 1563 2019-12-08T00:22:10Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less frequently and thus uncontrolled cell division would become less likely. Dinucleoside polyphosphates used as IMPDH inhibitors may contribute as anticancer and antiviral drugs<ref>PMID: 21517780</ref>.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structures/2'>IMPDH secondary structures</scene>. Alpha helices in pink. Beta sheets are in orange.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/2'>Impdh_quaternary_structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_space_fill/1'>Impdh_space_filled</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/2'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid red structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge since it is found in physiological environments. Positively and negatively charged amino acids play a part in intermediate covalent binding steps<ref>PMID: 31416831</ref>. <br /> <br /> <scene name='82/823087/Impdh_composition/1'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates and the affinity for those binded sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with Purine mononucleotides within the bateman domain. This requires the bateman domain to make IMPDH more sensitive to inhibition. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122631 Sandbox Reserved 1563 2019-12-08T00:15:03Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less frequently and thus uncontrolled cell division would become less likely. Dinucleoside polyphosphates used as IMPDH inhibitors may contribute as anticancer and antiviral drugs<ref>PMID: 21517780</ref>.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structures/2'>IMPDH secondary structures</scene>. Alpha helices in pink. Beta sheets are in orange.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/2'>Impdh_quaternary_structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_space_fill/1'>Impdh_space_filled</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/2'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid red structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge as this image shows. <br /> <br /> <scene name='82/823087/Impdh_composition/1'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates and the affinity for those binded sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with Purine mononucleotides within the bateman domain. This requires the bateman domain to make IMPDH more sensitive to inhibition. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122630 Sandbox Reserved 1563 2019-12-08T00:09:41Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer<ref>PMID: 31416831</ref>.<br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less and thus uncontrolled cell division would become less likely.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structures/2'>IMPDH secondary structures</scene>. Alpha helices in pink. Beta sheets are in orange.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/2'>Impdh_quaternary_structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_space_fill/1'>Impdh_space_filled</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/2'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid red structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge as this image shows. <br /> <br /> <scene name='82/823087/Impdh_composition/1'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates and the affinity for those binded sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with Purine mononucleotides within the bateman domain. This requires the bateman domain to make IMPDH more sensitive to inhibition. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> <br /> <references /></div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122620 Sandbox Reserved 1563 2019-12-07T23:52:13Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less and thus uncontrolled cell division would become less likely.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structures/2'>IMPDH secondary structures</scene>. Alpha helices in pink. Beta sheets are in orange.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/2'>Impdh_quaternary_structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_space_fill/1'>Impdh_space_filled</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/2'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid red structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge as this image shows. <br /> <br /> <scene name='82/823087/Impdh_composition/1'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates and the affinity for those binded sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with Purine mononucleotides within the bateman domain. This requires the bateman domain to make IMPDH more sensitive to inhibition. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122615 Sandbox Reserved 1563 2019-12-07T23:36:46Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less and thus uncontrolled cell division would become less likely.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structures/2'>IMPDH secondary structures</scene>. Alpha helices in pink. Beta sheets are in orange.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/2'>Impdh_quaternary_structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_space_filled/1'>IMPDH space filled view</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/2'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid red structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge as this image shows. <br /> <br /> <scene name='82/823087/Impdh_composition/1'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates and the affinity for those binded sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with Purine mononucleotides within the bateman domain. This requires the bateman domain to make IMPDH more sensitive to inhibition. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3122609 Sandbox Reserved 1563 2019-12-07T23:15:40Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less and thus uncontrolled cell division would become less likely.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structure/1'>IMPDH secondary structural features</scene>. Alpha helices in pink. Beta sheets are in orange.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/2'>Impdh_quaternary_structure</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_space_filled/1'>IMPDH space filled view</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/2'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid red structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge as this image shows. <br /> <br /> <scene name='82/823087/Impdh_composition/1'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates and the affinity for those binded sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with Purine mononucleotides within the bateman domain. This requires the bateman domain to make IMPDH more sensitive to inhibition. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118683 Sandbox Reserved 1563 2019-12-01T04:46:09Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less and thus uncontrolled cell division would become less likely.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structure/1'>IMPDH secondary structural features</scene>. Alpha helices in pink. Beta sheets are in orange.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/1'>IMPDH important quaternary structures</scene>. These quaternary structures include tetramers, compacted and extended octamers, and multiunit complexes. These are created through multiple subunits of tertiary structures. They are formed and reinforced through hydrogen bonding, disulfide bonds, and hydrophobic interactions. <br /> <br /> <scene name='82/823087/Impdh_space_filled/1'>IMPDH space filled view</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/2'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid red structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge as this image shows. <br /> <br /> <scene name='82/823087/Impdh_composition/1'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates and the affinity for those binded sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with Purine mononucleotides within the bateman domain. This requires the bateman domain to make IMPDH more sensitive to inhibition. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118681 Sandbox Reserved 1563 2019-12-01T04:40:23Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less and thus uncontrolled cell division would become less likely.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structure/1'>IMPDH secondary structural features</scene>. This view shows the N-terminus and C-terminus of the protein. Blue represents N-terminus. Red represents C-terminus.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/1'>IMPDH important quaternary structures</scene>. <br /> <br /> <scene name='82/823087/Impdh_space_filled/1'>IMPDH space filled view</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene>. For this image purple represent polar molecules and grey represents hydrophobic molecules.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/2'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid red structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge as this image shows. <br /> <br /> <scene name='82/823087/Impdh_composition/1'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> There are three binding sites within the bateman domain that regulate catalytic activity. These three sites bind dinucleoside polyphosphates and the affinity for those binded sites increases as activity with IMPDH increases. Purine dinucleoside polyphosphates compete with Purine mononucleotides within the bateman domain. This requires the bateman domain to make IMPDH more sensitive to inhibition. Covalent bonds are broken later in the reaction that allows the system enough energy to complete the process.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118675 Sandbox Reserved 1563 2019-12-01T04:22:24Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less and thus uncontrolled cell division would become less likely.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structure/1'>IMPDH secondary structural features</scene>. This view shows the N-terminus and C-terminus of the protein. Blue represents N-terminus. Red represents C-terminus.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/1'>IMPDH important quaternary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_space_filled/1'>IMPDH space filled view</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene>.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/2'>IMPDH ligand view</scene>. In this view the black structures are the ACT molecules. These are the ligands of the IMPDH protein.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid red structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge as this image shows. <br /> <br /> <scene name='82/823087/Impdh_composition/1'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118672 Sandbox Reserved 1563 2019-12-01T04:15:31Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less and thus uncontrolled cell division would become less likely.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structure/1'>IMPDH secondary structural features</scene>. This view shows the N-terminus and C-terminus of the protein. Blue represents N-terminus. Red represents C-terminus.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/1'>IMPDH important quaternary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_space_filled/1'>IMPDH space filled view</scene>. In the space filled view we can see a better representation of how much space the protein would actually take up. In the image the white is the protein as a whole and the red dots represent hydrogen bonds.<br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene>.<br /> <br /> <scene name='82/823087/Impdh_ligand_view/1'>IMPDH ligand view<br /> </scene>.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid red structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge as this image shows. <br /> <br /> <scene name='82/823087/Impdh_composition/1'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118668 Sandbox Reserved 1563 2019-12-01T04:12:15Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less and thus uncontrolled cell division would become less likely.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structure/1'>IMPDH secondary structural features</scene>. This view shows the N-terminus and C-terminus of the protein. Blue represents N-terminus. Red represents C-terminus.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/1'>IMPDH important quaternary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_space_filled/1'>IMPDH space filled view</scene>. <br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene><br /> <br /> <scene name='82/823087/Impdh_ligand_view/1'>IMPDH ligand view<br /> </scene>.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>. The IMPDH triad includes Arg (320), Asn (306), and Asp (272). This is represented by the solid red structures in the image. This triad is important as it makes cystine more reactive, which in turn induces binding.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>. The active binding cite is where the binding takes place after the catalytic triad makes cystine more reactive and binding is induced. In the image the cystines are in white. This is where binding would occur.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge as this image shows. <br /> <br /> <scene name='82/823087/Impdh_composition/1'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118665 Sandbox Reserved 1563 2019-12-01T03:59:10Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less and thus uncontrolled cell division would become less likely.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structure/1'>IMPDH secondary structural features</scene>. This view shows the N-terminus and C-terminus of the protein. Blue represents N-terminus. Red represents C-terminus.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/1'>IMPDH important quaternary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_space_filled/1'>IMPDH space filled view</scene>. <br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene><br /> <br /> <scene name='82/823087/Impdh_ligand_view/1'>IMPDH ligand view<br /> </scene>.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge as this image shows. <br /> <br /> <scene name='82/823087/Impdh_composition/1'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118664 Sandbox Reserved 1563 2019-12-01T03:56:24Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less and thus uncontrolled cell division would become less likely.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structure/1'>IMPDH secondary structural features</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/1'>IMPDH important quaternary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_space_filled/1'>IMPDH space filled view</scene>. <br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene><br /> <br /> <scene name='82/823087/Impdh_ligand_view/1'>IMPDH ligand view<br /> </scene>.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge as this image shows. <br /> <br /> <scene name='82/823087/Impdh_composition/1'>IMPDH composition</scene>. Brown represents a protein. Red represents a RNA. Green represents ligands.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118662 Sandbox Reserved 1563 2019-12-01T03:54:19Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less and thus uncontrolled cell division would become less likely.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structure/1'>IMPDH secondary structural features</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/1'>IMPDH important quaternary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_space_filled/1'>IMPDH space filled view</scene>. <br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene><br /> <br /> <scene name='82/823087/Impdh_ligand_view/1'>IMPDH ligand view<br /> </scene>.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>. IMPDH has no significant charge as this image shows. <br /> <br /> <scene name='82/823087/Impdh_composition/1'>IMPDH composition</scene>.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118657 Sandbox Reserved 1563 2019-12-01T03:43:03Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less and thus uncontrolled cell division would become less likely.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structure/1'>IMPDH secondary structural features</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/1'>IMPDH important quaternary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_space_filled/1'>IMPDH space filled view</scene>. <br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene><br /> <br /> <scene name='82/823087/Impdh_ligand_view/1'>IMPDH ligand view<br /> </scene>.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>.<br /> <br /> <scene name='82/823087/Impdh_composition/1'>IMPDH composition</scene>.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118655 Sandbox Reserved 1563 2019-12-01T03:37:07Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less and thus uncontrolled cell division would become less likely.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structure/1'>IMPDH secondary structural features</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/1'>IMPDH important quaternary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_space_filled/1'>IMPDH space filled view</scene>. <br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene><br /> <br /> <scene name='82/823087/Impdh_ligand_view/1'>IMPDH ligand view<br /> </scene>.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>.<br /> <br /> <br /> <br /> == '''Energy Transformation''' ==<br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118654 Sandbox Reserved 1563 2019-12-01T03:35:36Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer. <br /> Dinucleoside polyphosphates could allosterically regulate inhibition of IMPDH. If inhibition of IMPDH is regulated errors would occur less and thus uncontrolled cell division would become less likely.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structure/1'>IMPDH secondary structural features</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/1'>IMPDH important quaternary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_space_filled/1'>IMPDH space filled view</scene>. <br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene><br /> <br /> <scene name='82/823087/Impdh_ligand_view/1'>IMPDH ligand view<br /> </scene>.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>.<br /> <br /> <scene name='82/823087/Impdh_charge/1'>IMPDH charge</scene>.<br /> <br /> <br /> <br /> == '''Energy Transformation''' ==<br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118647 Sandbox Reserved 1563 2019-12-01T03:21:44Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structure/1'>IMPDH secondary structural features</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/1'>IMPDH important quaternary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_space_filled/1'>IMPDH space filled view</scene>. <br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene><br /> <br /> <scene name='82/823087/Impdh_ligand_view/1'>IMPDH ligand view<br /> </scene>.<br /> <br /> <scene name='82/823087/Impdh_triad/3'>IMPDH Triad</scene>.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118645 Sandbox Reserved 1563 2019-12-01T03:19:37Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structure/1'>IMPDH secondary structural features</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/1'>IMPDH important quaternary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_space_filled/1'>IMPDH space filled view</scene>. <br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene><br /> <br /> <scene name='82/823087/Impdh_ligand_view/1'>IMPDH ligand view<br /> </scene>.<br /> <br /> <scene name='82/823087/Impdh_triad_active_binding/1'>IMPDH active binding site</scene>.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118633 Sandbox Reserved 1563 2019-12-01T02:36:19Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> <scene name='82/823087/Impdh/1'>Inosine-5'-monophosphate dehydrogenase (IMPDH)</scene> catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structure/1'>IMPDH secondary structural features</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/1'>IMPDH important quaternary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_space_filled/1'>IMPDH space filled view</scene>. <br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene><br /> <br /> <scene name='82/823087/Impdh_ligand_view/1'>IMPDH ligand view<br /> </scene>.<br /> <br /> <br /> <br /> == '''Energy Transformation''' ==<br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118628 Sandbox Reserved 1563 2019-12-01T02:20:04Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> Inosine-5'-monophosphate dehydrogenase (IMPDH) catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structure/1'>IMPDH secondary structural features</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/1'>IMPDH important quaternary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_space_filled/1'>IMPDH space filled view</scene>. <br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene><br /> <br /> <scene name='82/823087/Impdh_ligand_view/1'>IMPDH ligand view<br /> </scene>.<br /> <br /> <br /> <br /> == '''Energy Transformation''' ==<br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118625 Sandbox Reserved 1563 2019-12-01T02:15:09Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> Inosine-5'-monophosphate dehydrogenase (IMPDH) catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structure/1'>IMPDH secondary structural features</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/1'>IMPDH important quaternary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_space_filled/1'>IMPDH space filled view.</scene>. <br /> <br /> <scene name='82/823087/Impdh_hydrophobicity/1'>IMPDH hydrophobicity view</scene><br /> <br /> == '''Energy Transformation''' ==<br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118619 Sandbox Reserved 1563 2019-12-01T02:10:38Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> Inosine-5'-monophosphate dehydrogenase (IMPDH) catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structure/1'>IMPDH secondary structural features</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/1'>IMPDH important quaternary structures</scene>.<br /> <br /> <scene name='82/823087/Impdh_space_filled/1'>IMPDH space filled view.</scene>. <br /> <br /> == '''Energy Transformation''' ==<br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118613 Sandbox Reserved 1563 2019-12-01T02:06:48Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> Inosine-5'-monophosphate dehydrogenase (IMPDH) catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structure/1'>IMPDH secondary structural features</scene>.<br /> <br /> <scene name='82/823087/Impdh_quaternary_structure/1'>IMPDH important quaternary structures</scene>.<br /> <br /> <br /> <br /> == '''Energy Transformation''' ==<br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118604 Sandbox Reserved 1563 2019-12-01T01:48:13Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> Inosine-5'-monophosphate dehydrogenase (IMPDH) catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> If IMPDH is not regulated correctly it could lead to uncontrolled cell division. Without the regulation of cell division this could lead to cancer.<br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <scene name='82/823087/Impdh_secondary_structure/1'>Main secondary structural features</scene>.<br /> <br /> == '''Energy Transformation''' ==<br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118600 Sandbox Reserved 1563 2019-12-01T01:33:19Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> <br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> Inosine-5'-monophosphate dehydrogenase (IMPDH) catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> <br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <br /> <br /> == '''Energy Transformation''' ==<br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118599 Sandbox Reserved 1563 2019-12-01T01:32:27Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> Inosine-5'-monophosphate dehydrogenase (IMPDH) catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <ref>31416831</ref><br /> <br /> == '''Broader Implications''' ==<br /> <br /> <br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <br /> <br /> == '''Energy Transformation''' ==<br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118597 Sandbox Reserved 1563 2019-12-01T01:22:21Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> Inosine-5'-monophosphate dehydrogenase (IMPDH) catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). Additional ligands include Acetate (ACT) and Guanosine-5'-monophosphate (5GP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. IMPDH is used medically to help fight against microbial infections and cancer. <br /> <br /> == '''Broader Implications''' ==<br /> <br /> <br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <br /> <br /> == '''Energy Transformation''' ==<br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118591 Sandbox Reserved 1563 2019-12-01T01:09:40Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='6rpu' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> Inosine-5'-monophosphate dehydrogenase (IMPDH) catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. <br /> <br /> == '''Broader Implications''' ==<br /> <br /> <br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <br /> <br /> == '''Energy Transformation''' ==<br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow https://proteopedia.org/index.php?title=Sandbox_Reserved_1563&diff=3118588 Sandbox Reserved 1563 2019-12-01T01:07:10Z

<p>Garrett Leibow: </p> <hr /> <div>{{Sandbox_Reserved_BHall_Chem351_F19}}<br /> =='''Inosine-5'-monophosphate dehydrogenase (IMPDH)'''==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == '''Function(s) and Biological Relevance''' ==<br /> <br /> Inosine-5'-monophosphate dehydrogenase (IMPDH) catalyzes the rate limiting step of the de novo guanine nucleotide biosynthetic pathway. NAD is reduced resulting in IMP converting to Xanthosine monophosphate (XMP). IMPDH is found in organisms that go through the purine biosynthetic pathway, this includes humans. <br /> <br /> == '''Broader Implications''' ==<br /> <br /> <br /> <br /> == '''Structural highlights and structure-function relationships''' ==<br /> <br /> <br /> <br /> == '''Energy Transformation''' ==<br /> <br /> <br /> <br /> This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> </StructureSection><br /> == References ==<br /> 1. Fernández-Justel, D.; Peláez, R.; Revuelta, J. L.; Buey, R. M. The Bateman Domain of IMP Dehydrogenase Is a Binding Target for Dinucleoside Polyphosphates. J Biol Chem 2019, 294 (40), 14768–14775.</div>

Garrett Leibow