https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Steve+KlimcakProteopedia - User contributions [en]2026-10-02T18:14:35ZUser contributionsMediaWiki 1.43.8https://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3033862User:Steve Klimcak/Sandbox 12019-04-25T18:42:39Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The demethylation of lysine via LSD1 occurs through oxidation via a hydride transfer. Shown in Figure 2 the first step involves the <scene name='81/811710/Fad_highlight/1'>Flavin Adenine Dinucleotide cofactor</scene> initiating a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. The FAD co-factor is also negatively charged and lysine residue 661 provides stability by drawing that charge away. In the next step the imine is hydrolyzed and transitions to an hemiaminal. This then breaks down to formaldehyde and the product lysine. <br />
[[Image:LSD1Mech2.jpg|400px|right|thumb|Figure 2]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. These residues in the <scene name='81/811712/Hydrophobic_pocket/4'>hydrophobic pocket</scene> shown in green surrounds the FAD in a way such that it exposes the catalytic nitrogen(N5) that is responsible for the two electron demethylation. The <scene name='81/811712/Fad_n5/3'>catalytic nitrogen</scene> depicted as a sphere is approximately 3.5Å away from the substrate lysine. Lysine 661 shown 4.98Å is responsible for anchoring the FAD in place to efficiently bind the substrate lysine. A structure complex of LSD1 with the a substrate lysine encased in has yet to be crystallized. Another three seperate pockets help bind the histone tail residues to the substrate lysine which is essential for identifying different modifications of the histone tail.<br />
<br />
==Application==<br />
LSD1 plays a pivital role in many biological processes such as cell growth, epithelial-mesenchymal transition, stem cell biology, malignant transformation of cells, and cell differentiation. Malfunctioning of these processes can lead to life threatening diseases including but not limited to myeloid leukemia and acute lymphoblastic leukemia. Evidence has shown that these activities have ties to prostate and small cell lung cancer so studies have been done to find a reliable inhibitor for LSD1. Monamine oxidases utilize the FAD co-factor much like LSD1 and inhibitors of monamaine oxidase have proven to be successful in inhibiting the activity of LSD1. A patent for 5-cyano indole derivatives(compound similar in structure to monoamine oxidase inhibitors) has been proposed to be a potential inhibitor for LSD1. More specifically trans-2-Phenylcyclopropylamine has been shown the best representation of this inhibition. The formation of a product via an addition reaction through the flavin ring can restrict LSD1's activity with subsequent one‐electron oxidation and cyclopropyl ring opening. However due to the selective nature of 2-PCPA it does not present a strong enough affinity for LSD1's activity. Alternative structures using the foundation of 2-PCPA are continually being researched to find the best fit inhibitor for LSD1. An article published in Wiley Online Library discusses a number of potential LSD1 inhibitors based on monoamine oxidase inhibitors [https://onlinelibrary.wiley.com/doi/full/10.1002/med.21350]. Thus inhibition of LSD1 opens new pathways for possible treatments for cancers and disorders.<br />
[[Image:FAD-PCPA.jpg|400px|right|thumb|Figure 2]]<br />
<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<ref name="Abdel-Magid">PMID:29152043</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3033861User:Steve Klimcak/Sandbox 12019-04-25T18:40:47Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The demethylation of lysine via LSD1 occurs through oxidation via a hydride transfer. Shown in Figure 2 the first step involves the <scene name='81/811710/Fad_highlight/1'>Flavin Adenine Dinucleotide cofactor</scene> initiating a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. The FAD co-factor is also negatively charged and lysine residue 661 provides stability by drawing that charge away. In the next step the imine is hydrolyzed and transitions to an hemiaminal. This then breaks down to formaldehyde and the product lysine. <br />
[[Image:LSD1Mech2.jpg|400px|right|thumb|Figure 2]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. These residues in the <scene name='81/811712/Hydrophobic_pocket/4'>hydrophobic pocket</scene> shown in green surrounds the FAD in a way such that it exposes the catalytic nitrogen(N5) that is responsible for the two electron demethylation. The <scene name='81/811712/Fad_n5/3'>catalytic nitrogen</scene> depicted as a sphere is approximately 3.5Å away from the substrate lysine. Lysine 661 shown 4.98Å is responsible for anchoring the FAD in place to efficiently bind the substrate lysine. A structure complex of LSD1 with the a substrate lysine encased in has yet to be crystallized. Another three seperate pockets help bind the histone tail residues to the substrate lysine which is essential for identifying different modifications of the histone tail.<br />
<br />
==Application==<br />
LSD1 plays a pivital role in many biological processes such as cell growth, epithelial-mesenchymal transition, stem cell biology, malignant transformation of cells, and cell differentiation. Malfunctioning of these processes can lead to life threatening diseases including but not limited to myeloid leukemia and acute lymphoblastic leukemia. Evidence has shown that these activities have ties to prostate and small cell lung cancer so studies have been done to find a reliable inhibitor for LSD1. Monamine oxidases utilize the FAD co-factor much like LSD1 and inhibitors of monamaine oxidase have proven to be successful in inhibiting the activity of LSD1. A patent for 5-cyano indole derivatives(compound similar in structure to monoamine oxidase inhibitors) has been proposed to be a potential inhibitor for LSD1. More specifically trans-2-Phenylcyclopropylamine has been shown the best representation of this inhibition. The formation of a product via an addition reaction through the flavin ring can restrict LSD1's activity with subsequent one‐electron oxidation and cyclopropyl ring opening. However due to the selective nature of 2-PCPA it does not present a strong enough affinity for LSD1's activity. Alternative structures using the foundation of 2-PCPA are continually being researched to find the best fit inhibitor for LSD1. An article published in Wiley Online Library discusses a number of potential LSD1 inhibitors based on monoamine oxidase inhibitors. Thus inhibition of LSD1 opens new pathways for possible treatments for cancers and disorders.<br />
[[Image:FAD-PCPA.jpg|400px|right|thumb|Figure 2]]<br />
<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<ref name="Abdel-Magid">PMID:29152043</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=File:FAD-PCPA.jpg&diff=3033860File:FAD-PCPA.jpg2019-04-25T18:39:36Z<p>Steve Klimcak: The product formed to inhibit LSD1's activity.</p>
<hr />
<div>The product formed to inhibit LSD1's activity.</div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3033859User:Steve Klimcak/Sandbox 12019-04-25T18:38:09Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The demethylation of lysine via LSD1 occurs through oxidation via a hydride transfer. Shown in Figure 2 the first step involves the <scene name='81/811710/Fad_highlight/1'>Flavin Adenine Dinucleotide cofactor</scene> initiating a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. The FAD co-factor is also negatively charged and lysine residue 661 provides stability by drawing that charge away. In the next step the imine is hydrolyzed and transitions to an hemiaminal. This then breaks down to formaldehyde and the product lysine. <br />
[[Image:LSD1Mech2.jpg|400px|right|thumb|Figure 2]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. These residues in the <scene name='81/811712/Hydrophobic_pocket/4'>hydrophobic pocket</scene> shown in green surrounds the FAD in a way such that it exposes the catalytic nitrogen(N5) that is responsible for the two electron demethylation. The <scene name='81/811712/Fad_n5/3'>catalytic nitrogen</scene> depicted as a sphere is approximately 3.5Å away from the substrate lysine. Lysine 661 shown 4.98Å is responsible for anchoring the FAD in place to efficiently bind the substrate lysine. A structure complex of LSD1 with the a substrate lysine encased in has yet to be crystallized. Another three seperate pockets help bind the histone tail residues to the substrate lysine which is essential for identifying different modifications of the histone tail.<br />
<br />
==Application==<br />
LSD1 plays a pivital role in many biological processes such as cell growth, epithelial-mesenchymal transition, stem cell biology, malignant transformation of cells, and cell differentiation. Malfunctioning of these processes can lead to life threatening diseases including but not limited to myeloid leukemia and acute lymphoblastic leukemia. Evidence has shown that these activities have ties to prostate and small cell lung cancer so studies have been done to find a reliable inhibitor for LSD1. Monamine oxidases utilize the FAD co-factor much like LSD1 and inhibitors of monamaine oxidase have proven to be successful in inhibiting the activity of LSD1. A patent for 5-cyano indole derivatives(compound similar in structure to monoamine oxidase inhibitors) has been proposed to be a potential inhibitor for LSD1. More specifically trans-2-Phenylcyclopropylamine has been shown the best representation of this inhibition. The formation of a product via an addition reaction through the flavin ring can restrict LSD1's activity with subsequent one‐electron oxidation and cyclopropyl ring opening. However due to the selective nature of 2-PCPA it does not present a strong enough affinity for LSD1's activity. Alternative structures using the foundation of 2-PCPA are continually being researched to find the best fit inhibitor for LSD1. An article published in Wiley Online Library discusses a number of potential LSD1 inhibitors based on monoamine oxidase inhibitors. Thus inhibition of LSD1 opens new pathways for possible treatments for cancers and disorders.<br />
<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<ref name="Abdel-Magid">PMID:29152043</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3033846User:Steve Klimcak/Sandbox 12019-04-25T16:48:23Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The demethylation of lysine via LSD1 occurs through oxidation via a hydride transfer. Shown in Figure 2 the first step involves the <scene name='81/811710/Fad_highlight/1'>Flavin Adenine Dinucleotide cofactor</scene> initiating a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. The FAD co-factor is also negatively charged and lysine residue 661 provides stability by drawing that charge away. In the next step the imine is hydrolyzed and transitions to an hemiaminal. This then breaks down to formaldehyde and the product lysine. <br />
[[Image:LSD1Mech2.jpg|400px|right|thumb|Figure 2]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. These residues in the <scene name='81/811712/Hydrophobic_pocket/4'>hydrophobic pocket</scene> shown in green surrounds the FAD in a way such that it exposes the catalytic nitrogen(N5) that is responsible for the two electron demethylation. The <scene name='81/811712/Fad_n5/3'>catalytic nitrogen</scene> depicted as a sphere is approximately 3.5Å away from the substrate lysine. Lysine 661 shown 4.98Å is responsible for anchoring the FAD in place to efficiently bind the substrate lysine. A structure complex of LSD1 with the a substrate lysine encased in has yet to be crystallized. Another three seperate pockets help bind the histone tail residues to the substrate lysine which is essential for identifying different modifications of the histone tail.<br />
<br />
==Application==<br />
LSD1 plays a pivital role in many biological processes such as cell growth, epithelial-mesenchymal transition, stem cell biology, malignant transformation of cells, and cell differentiation. Malfunctioning of these activities can lead to life threatening diseases such as acute myeloid leukemia and acute lymphoblastic leukemia. Evidence has shown that these activities have ties to prostate and small cell lung cancer so studies have been done to find a reliable inhibitor for LSD1. Monamine oxidases utilize the FAD co-factor much like LSD1 and inhibitors of monamaine oxidase have proven to be successful in inhibiting the activity of LSD1. Thus inhibition of LSD1 opens new pathways for possible treatments for cancers and disorders.<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<ref name="Abdel-Magid">PMID:29152043</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3033843User:Steve Klimcak/Sandbox 12019-04-25T16:41:35Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The demethylation of lysine via LSD1 occurs through oxidation via a hydride transfer. Shown in Figure 2 the first step involves the <scene name='81/811710/Fad_highlight/1'>Flavin Adenine Dinucleotide cofactor</scene> initiating a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. The FAD co-factor is also negatively charged and lysine residue 661 provides stability by drawing that charge away. In the next step the imine is hydrolyzed and transitions to an hemiaminal. This then breaks down to formaldehyde and the product lysine. <br />
[[Image:LSD1Mech2.jpg|400px|right|thumb|Figure 2]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. These residues in the <scene name='81/811712/Hydrophobic_pocket/4'>hydrophobic pocket</scene> shown in green surrounds the FAD in a way such that it exposes the catalytic nitrogen(N5) that is responsible for the two electron demethylation. The <scene name='81/811712/Fad_n5/3'>catalytic nitrogen</scene> depicted as a sphere is approximately 3.5Å away from the substrate lysine. Lysine 661 shown 4.98Å is responsible for anchoring the FAD in place to efficiently bind the substrate lysine. Another three seperate pockets help bind the histone tail residues to the substrate lysine which is essential for identifying different modifications of the histone tail.<br />
<br />
==Application==<br />
LSD1 plays a pivital role in many biological processes such as cell growth, epithelial-mesenchymal transition, stem cell biology, malignant transformation of cells, and cell differentiation. Malfunctioning of these activities can lead to life threatening diseases such as acute myeloid leukemia and acute lymphoblastic leukemia. Evidence has shown that these activities have ties to prostate and small cell lung cancer so studies have been done to find a reliable inhibitor for LSD1. Monamine oxidases utilize the FAD co-factor much like LSD1 and inhibitors of monamaine oxidase have proven to be successful in inhibiting the activity of LSD1. Thus inhibition of LSD1 opens new pathways for possible treatments for cancers and disorders.<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<ref name="Abdel-Magid">PMID:29152043</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3030258User:Steve Klimcak/Sandbox 12019-04-23T18:27:50Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The demethylation of lysine via LSD1 occurs through oxidation via a hydride transfer. Shown in Figure 2 the first step involves the <scene name='81/811710/Fad_highlight/1'>Flavin Adenine Dinucleotide cofactor</scene> initiating a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. The FAD co-factor is also negatively charged and lysine residue 661 provides stability by drawing that charge away. In the next step the imine is hydrolyzed and transitions to an hemiaminal. This then breaks down to formaldehyde and the product lysine. <br />
[[Image:LSD1Mech2.jpg|400px|right|thumb|Figure 2]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. These residues in the <scene name='81/811712/Hydrophobic_pocket/1'>hydrophobic pocket</scene> shown in green surrounds the FAD in a way such that it exposes the catalytic nitrogen(N5) that is responsible for the two electron demethylation. The <scene name='81/811712/Fad_n5/3'>catalytic nitrogen</scene> depicted as a sphere is approximately 3.5Å away from the substrate lysine. Lysine 661 shown 4.98Å is responsible for anchoring the FAD in place to efficiently bind the substrate lysine. Another three seperate pockets help bind the histone tail residues to the substrate lysine which is essential for identifying different modifications of the histone tail.<br />
<br />
==Application==<br />
LSD1 plays a pivital role in many biological processes such as cell growth, epithelial-mesenchymal transition, stem cell biology, malignant transformation of cells, and cell differentiation. Malfunctioning of these activities can lead to life threatening diseases such as acute myeloid leukemia and acute lymphoblastic leukemia. Evidence has shown that these activities have ties to prostate and small cell lung cancer so studies have been done to find a reliable inhibitor for LSD1. Monamine oxidases utilize the FAD co-factor much like LSD1 and inhibitors of monamaine oxidase have proven to be successful in inhibiting the activity of LSD1. Thus inhibition of LSD1 opens new pathways for possible treatments for cancers and disorders.<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<ref name="Abdel-Magid">PMID:29152043</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=File:LSD1Mech2.jpg&diff=3030257File:LSD1Mech2.jpg2019-04-23T18:26:53Z<p>Steve Klimcak: </p>
<hr />
<div></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3029906User:Steve Klimcak/Sandbox 12019-04-19T18:12:57Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The demethylation of lysine via LSD1 occurs through oxidation via a hydride transfer. Shown in Figure 2 the first step involves the <scene name='81/811710/Fad_highlight/1'>Flavin Adenine Dinucleotide cofactor</scene> initiating a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. The FAD co-factor is also negatively charged and lysine residue 661 provides stability by drawing that charge away. In the next step the imine is hydrolyzed and transitions to an hemiaminal. This then breaks down to formaldehyde and the product lysine. <br />
[[Image:LSD1 Mech1.jpg|400px|right|thumb|Figure 2]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. These residues in the <scene name='81/811712/Hydrophobic_pocket/1'>hydrophobic pocket</scene> shown in green surrounds the FAD in a way such that it exposes the catalytic nitrogen(N5) that is responsible for the two electron demethylation. The <scene name='81/811712/Fad_n5/3'>catalytic nitrogen</scene> depicted as a sphere is approximately 3.5Å away from the substrate lysine. Lysine 661 shown 4.98Å is responsible for anchoring the FAD in place to efficiently bind the substrate lysine. Another three seperate pockets help bind the histone tail residues to the substrate lysine which is essential for identifying different modifications of the histone tail.<br />
<br />
==Application==<br />
LSD1 plays a pivital role in many biological processes such as cell growth, epithelial-mesenchymal transition, stem cell biology, malignant transformation of cells, and cell differentiation. Malfunctioning of these activities can lead to life threatening diseases such as acute myeloid leukemia and acute lymphoblastic leukemia. Evidence has shown that these activities have ties to prostate and small cell lung cancer so studies have been done to find a reliable inhibitor for LSD1. Monamine oxidases utilize the FAD co-factor much like LSD1 and inhibitors of monamaine oxidase have proven to be successful in inhibiting the activity of LSD1. Thus inhibition of LSD1 opens new pathways for possible treatments for cancers and disorders.<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<ref name="Abdel-Magid">PMID:29152043</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=File:LSD1_Mech1.jpg&diff=3029905File:LSD1 Mech1.jpg2019-04-19T18:11:05Z<p>Steve Klimcak: Figure 2</p>
<hr />
<div>Figure 2</div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3029897User:Steve Klimcak/Sandbox 12019-04-19T17:51:47Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The demethylation of lysine via LSD1 occurs through oxidation via a hydride transfer. Shown in Figure 2 the first step involves the <scene name='81/811710/Fad_highlight/1'>Flavin Adenine Dinucleotide cofactor</scene> initiating a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. The FAD co-factor is also negatively charged and lysine residue 661 provides stability by drawing that charge away. In the next step the imine is hydrolyzed and transitions to an hemiaminal. This then breaks down to formaldehyde and the product lysine. <br />
[[Image:LSD1 Mech.jpg|400px|right|thumb|Figure 2]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. These residues in the <scene name='81/811712/Hydrophobic_pocket/1'>hydrophobic pocket</scene> shown in green surrounds the FAD in a way such that it exposes the catalytic nitrogen(N5) that is responsible for the two electron demethylation. The <scene name='81/811712/Fad_n5/3'>catalytic nitrogen</scene> depicted as a sphere is approximately 3.5Å away from the substrate lysine. Lysine 661 shown 4.98Å is responsible for anchoring the FAD in place to efficiently bind the substrate lysine. Another three seperate pockets help bind the histone tail residues to the substrate lysine which is essential for identifying different modifications of the histone tail.<br />
<br />
==Application==<br />
LSD1 plays a pivital role in many biological processes such as cell growth, epithelial-mesenchymal transition, stem cell biology, malignant transformation of cells, and cell differentiation. Malfunctioning of these activities can lead to life threatening diseases such as acute myeloid leukemia and acute lymphoblastic leukemia. Evidence has shown that these activities have ties to prostate and small cell lung cancer so studies have been done to find a reliable inhibitor for LSD1. Monamine oxidases utilize the FAD co-factor much like LSD1 and inhibitors of monamaine oxidase have proven to be successful in inhibiting the activity of LSD1. Thus inhibition of LSD1 opens new pathways for possible treatments for cancers and disorders.<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<ref name="Abdel-Magid">PMID:29152043</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3029895User:Steve Klimcak/Sandbox 12019-04-19T17:48:50Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The demethylation of lysine via LSD1 occurs through oxidation via a hydride transfer. Shown in Figure 2 the first step involves the <scene name='81/811710/Fad_highlight/1'>Flavin Adenine Dinucleotide cofactor</scene> initiating a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. The FAD co-factor is also negatively charged and lysine residue 661 provides stability by drawing that charge away. In the next step the imine is hydrolyzed and transitions to an hemiaminal. This then breaks down to formaldehyde and the product lysine. <br />
[[Image:LSD1 Mech.jpg|400px|right|thumb|Figure 2]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. These residues in the <scene name='81/811712/Hydrophobic_pocket/1'>hydrophobic pocket</scene> shown in green surrounds the FAD in a way such that it exposes the catalytic nitrogen(N5) that is responsible for the two electron demethylation. The <scene name='81/811712/Fad_n5/2'>catalytic nitrogen</scene> depicted as a sphere is approximately 3.5Å away from the substrate lysine. Lysine 661 shown 4.98Å is responsible for anchoring the FAD in place to efficiently bind the substrate lysine. Another three seperate pockets help bind the histone tail residues to the substrate lysine which is essential for identifying different modifications of the histone tail.<br />
<br />
==Application==<br />
LSD1 plays a pivital role in many biological processes such as cell growth, epithelial-mesenchymal transition, stem cell biology, malignant transformation of cells, and cell differentiation. Malfunctioning of these activities can lead to life threatening diseases such as acute myeloid leukemia and acute lymphoblastic leukemia. Evidence has shown that these activities have ties to prostate and small cell lung cancer so studies have been done to find a reliable inhibitor for LSD1. Monamine oxidases utilize the FAD co-factor much like LSD1 and inhibitors of monamaine oxidase have proven to be successful in inhibiting the activity of LSD1. Thus inhibition of LSD1 opens new pathways for possible treatments for cancers and disorders.<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<ref name="Abdel-Magid">PMID:29152043</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3029872User:Steve Klimcak/Sandbox 12019-04-19T17:09:52Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The demethylation of lysine via LSD1 occurs through oxidation via a hydride transfer. Shown in Figure 2 the first step involves the <scene name='81/811710/Fad_highlight/1'>Flavin Adenine Dinucleotide cofactor</scene> initiating a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. The FAD co-factor is also negatively charged and lysine residue 661 provides stability by drawing that charge away. In the next step the imine is hydrolyzed and transitions to an hemiaminal. This then breaks down to formaldehyde and the product lysine. <br />
[[Image:LSD1 Mech.jpg|400px|right|thumb|Figure 2]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. These residues in the <scene name='81/811712/Hydrophobic_pocket/1'>hydrophobic pocket</scene> shown in green surrounds the FAD in a way such that it exposes the catalytic nitrogen(N5) that is responsible for the two electron demethylation. The <scene name='81/811712/Fad_n5/1'>catalytic nitrogen</scene> depicted as a sphere is approximately 3.5Å away from the substrate lysine. Another three seperate pockets help bind the histone tail residues to the substrate lysine which is essential for identifying different modifications of the histone tail.<br />
<br />
==Application==<br />
LSD1 plays a pivital role in many biological processes such as cell growth, epithelial-mesenchymal transition, stem cell biology, malignant transformation of cells, and cell differentiation. Malfunctioning of these activities can lead to life threatening diseases such as acute myeloid leukemia and acute lymphoblastic leukemia. Evidence has shown that these activities have ties to prostate and small cell lung cancer so studies have been done to find a reliable inhibitor for LSD1. Monamine oxidases utilize the FAD co-factor much like LSD1 and inhibitors of monamaine oxidase have proven to be successful in inhibiting the activity of LSD1. Thus inhibition of LSD1 opens new pathways for possible treatments for cancers and disorders.<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<ref name="Abdel-Magid">PMID:29152043</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3029868User:Steve Klimcak/Sandbox 12019-04-19T17:08:54Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The demethylation of lysine via LSD1 occurs through oxidation via a hydride transfer. Shown in Figure 2 the first step involves the <scene name='81/811710/Fad_highlight/1'>Flavin Adenine Dinucleotide cofactor</scene> initiating a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. The FAD co-factor is also negatively charged and lysine residue 661 provides stability by drawing that charge away. In the next step the imine is hydrolyzed and transitions to an hemiaminal. This then breaks down to formaldehyde and the product lysine. <br />
[[Image:LSD1 Mech.jpg|400px|right|thumb|Figure 2]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. These residues in the <scene name='81/811712/Hydrophobic_pocket/1'>hydrophobic pocket</scene> shown in green surrounds the FAD in a way such that it exposes the catalytic nitrogen(N5) that is responsible for the two electron demethylation. The <scene name='81/811712/Fad_n5/1'>catalytic nitrogen</scene> depicted as a sphere is approximately 3.5Å away from the substrate lysine which through its imine intermediate can stabilize the negative charge on the FAD. Another three seperate pockets help bind the histone tail residues to the substrate lysine which is essential for identifying different modifications of the histone tail.<br />
<br />
==Application==<br />
LSD1 plays a pivital role in many biological processes such as cell growth, epithelial-mesenchymal transition, stem cell biology, malignant transformation of cells, and cell differentiation. Malfunctioning of these activities can lead to life threatening diseases such as acute myeloid leukemia and acute lymphoblastic leukemia. Evidence has shown that these activities have ties to prostate and small cell lung cancer so studies have been done to find a reliable inhibitor for LSD1. Monamine oxidases utilize the FAD co-factor much like LSD1 and inhibitors of monamaine oxidase have proven to be successful in inhibiting the activity of LSD1. Thus inhibition of LSD1 opens new pathways for possible treatments for cancers and disorders.<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<ref name="Abdel-Magid">PMID:29152043</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3029855User:Steve Klimcak/Sandbox 12019-04-18T21:34:08Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The demethylation of lysine via LSD1 occurs through oxidation via a hydride transfer. Shown in Figure 2 the first step involves the <scene name='81/811710/Fad_highlight/1'>Flavin Adenine Dinucleotide cofactor</scene> initiating a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. The FAD co-factor is also negatively charged and the imine cation could provide stability by drawing that charge away. In the next step the imine is hydrolyzed and transitions to an hemiaminal. This then breaks down to formaldehyde and the product lysine. <br />
[[Image:LSD1 Mech.jpg|400px|right|thumb|Figure 2]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. These residues in the <scene name='81/811712/Hydrophobic_pocket/1'>hydrophobic pocket</scene> shown in green surrounds the FAD in a way such that it exposes the catalytic nitrogen(N5) that is responsible for the two electron demethylation. The <scene name='81/811712/Fad_n5/1'>catalytic nitrogen</scene> depicted as a sphere is approximately 3.5Å away from the substrate lysine which through its imine intermediate can stabilize the negative charge on the FAD. Another three seperate pockets help bind the histone tail residues to the substrate lysine which is essential for identifying different modifications of the histone tail.<br />
<br />
==Application==<br />
LSD1 plays a pivital role in many biological processes such as cell growth, epithelial-mesenchymal transition, stem cell biology, malignant transformation of cells, and cell differentiation. Malfunctioning of these activities can lead to life threatening diseases such as acute myeloid leukemia and acute lymphoblastic leukemia. Evidence has shown that these activities have ties to prostate and small cell lung cancer so studies have been done to find a reliable inhibitor for LSD1. Monamine oxidases utilize the FAD co-factor much like LSD1 and inhibitors of monamaine oxidase have proven to be successful in inhibiting the activity of LSD1. Thus inhibition of LSD1 opens new pathways for possible treatments for cancers and disorders.<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<ref name="Abdel-Magid">PMID:29152043</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3029854User:Steve Klimcak/Sandbox 12019-04-18T21:33:30Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The demethylation of lysine via LSD1 occurs through oxidation via a hydride transfer. Shown in Figure 2 the first step involves the <scene name='81/811710/Fad_highlight/1'>Flavin Adenine Dinucleotide cofactor</scene> initiating a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. The FAD co-factor is also negatively charged and the imine cation could provide stability by drawing that charge away. In the next step the imine is hydrolyzed and transitions to an hemiaminal. This then breaks down to formaldehyde and the product lysine. <br />
[[Image:LSD1 Mech.jpg|400px|right|thumb|Figure 2]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. These residues in the <scene name='81/811712/Hydrophobic_pocket/1'>hydrophobic pocket</scene> shown in green surrounds the FAD in a way such that it exposes the catalytic nitrogen(N5) that is responsible for the two electron demethylation. The <scene name='81/811712/Fad_n5/1'>catalytic nitrogen</scene> depicted as a sphere is approximately 3.5Å away from the substrate lysine which trough its imine intermediate can stabilize the negative charge on the FAD. Another three seperate pockets help bind the histone tail residues to the substrate lysine which is essential for identifying different modifications of the histone tail.<br />
<br />
==Application==<br />
LSD1 plays a pivital role in many biological processes such as cell growth, epithelial-mesenchymal transition, stem cell biology, malignant transformation of cells, and cell differentiation. Malfunctioning of these activities can lead to life threatening diseases such as acute myeloid leukemia and acute lymphoblastic leukemia. Evidence has shown that these activities have ties to prostate and small cell lung cancer so studies have been done to find a reliable inhibitor for LSD1. Monamine oxidases utilize the FAD co-factor much like LSD1 and inhibitors of monamaine oxidase have proven to be successful in inhibiting the activity of LSD1. Thus inhibition of LSD1 opens new pathways for possible treatments for cancers and disorders.<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<ref name="Abdel-Magid">PMID:29152043</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3029853User:Steve Klimcak/Sandbox 12019-04-18T21:04:11Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The demethylation of lysine via LSD1 occurs through oxidation via a hydride transfer. Shown in Figure 2 the first step involves the <scene name='81/811710/Fad_highlight/1'>Flavin Adenine Dinucleotide cofactor</scene> initiating a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. The FAD co-factor is also negatively charged and the imine cation could provide stability by drawing that charge away. In the next step the imine is hydrolyzed and transitions to an hemiaminal. This then breaks down to formaldehyde and the product lysine. <br />
[[Image:LSD1 Mech.jpg|400px|right|thumb|Figure 2]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. These residues in the <scene name='81/811712/Hydrophobic_pocket/1'>hydrophobic pocket</scene> shown in green surrounds the FAD in a way such that it exposes the <scene name='81/811710/Fad_n5/4'>catalytic nitrogen(N5)</scene> that is responsible for the two electron demethylation. Another three seperate pockets help bind the histone tail residues to the substrate lysine which is essential for identifying different modifications of the histone tail.<br />
<br />
==Application==<br />
LSD1 plays a pivital role in many biological processes such as cell growth, epithelial-mesenchymal transition, stem cell biology, malignant transformation of cells, and cell differentiation. Malfunctioning of these activities can lead to life threatening diseases such as acute myeloid leukemia and acute lymphoblastic leukemia. Evidence has shown that these activities have ties to prostate and small cell lung cancer so studies have been done to find a reliable inhibitor for LSD1. Monamine oxidases utilize the FAD co-factor much like LSD1 and inhibitors of monamaine oxidase have proven to be successful in inhibiting the activity of LSD1. Thus inhibition of LSD1 opens new pathways for possible treatments for cancers and disorders.<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<ref name="Abdel-Magid">PMID:29152043</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3029852User:Steve Klimcak/Sandbox 12019-04-18T21:03:47Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The demethylation of lysine via LSD1 occurs through oxidation via a hydride transfer. Shown in Figure 2 the first step involves the <scene name='81/811710/Fad_highlight/1'>Flavin Adenine Dinucleotide cofactor</scene> initiating a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. The FAD co-factor is also negatively charged and the imine cation could provide stability by drawing that charge away. In the next step the imine is hydrolyzed and transitions to an hemiaminal. This then breaks down to formaldehyde and the product lysine. <br />
[[Image:LSD1 Mech.jpg|400px|right|thumb|Figure 2]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. These residues in he <scene name='81/811712/Hydrophobic_pocket/1'>hydrophobic pocket</scene> shown in green surrounds the FAD in a way such that it exposes the <scene name='81/811710/Fad_n5/4'>catalytic nitrogen(N5)</scene> that is responsible for the two electron demethylation. Another three seperate pockets help bind the histone tail residues to the substrate lysine which is essential for identifying different modifications of the histone tail.<br />
<br />
==Application==<br />
LSD1 plays a pivital role in many biological processes such as cell growth, epithelial-mesenchymal transition, stem cell biology, malignant transformation of cells, and cell differentiation. Malfunctioning of these activities can lead to life threatening diseases such as acute myeloid leukemia and acute lymphoblastic leukemia. Evidence has shown that these activities have ties to prostate and small cell lung cancer so studies have been done to find a reliable inhibitor for LSD1. Monamine oxidases utilize the FAD co-factor much like LSD1 and inhibitors of monamaine oxidase have proven to be successful in inhibiting the activity of LSD1. Thus inhibition of LSD1 opens new pathways for possible treatments for cancers and disorders.<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<ref name="Abdel-Magid">PMID:29152043</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3029851User:Steve Klimcak/Sandbox 12019-04-18T20:31:46Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The demethylation of lysine via LSD1 occurs through oxidation via a hydride transfer. Shown in Figure 2 the first step involves the <scene name='81/811710/Fad_highlight/1'>Flavin Adenine Dinucleotide cofactor</scene> initiating a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. The FAD co-factor is also negatively charged and the imine cation could provide stability by drawing that charge away. In the next step the imine is hydrolyzed and transitions to an hemiaminal. This then breaks down to formaldehyde and the product lysine. <br />
[[Image:LSD1 Mech.jpg|400px|right|thumb|Figure 2]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. The <scene name='81/811712/Hydrophobic_pocket/1'>hydrophobic pocket</scene> shown in green surrounds the FAD in a way such that it exposes the <scene name='81/811710/Fad_n5/4'>catalytic nitrogen(N5)</scene> that is responsible for the two electron demethylation. Another three seperate pockets help bind the histone tail residues to the substrate lysine which is essential for identifying different modifications of the histone tail.<br />
<br />
==Application==<br />
LSD1 plays a pivital role in many biological processes such as cell growth, epithelial-mesenchymal transition, stem cell biology, malignant transformation of cells, and cell differentiation. Malfunctioning of these activities can lead to life threatening diseases such as acute myeloid leukemia and acute lymphoblastic leukemia. Evidence has shown that these activities have ties to prostate and small cell lung cancer so studies have been done to find a reliable inhibitor for LSD1. Monamine oxidases utilize the FAD co-factor much like LSD1 and inhibitors of monamaine oxidase have proven to be successful in inhibiting the activity of LSD1. Thus inhibition of LSD1 opens new pathways for possible treatments for cancers and disorders.<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<ref name="Abdel-Magid">PMID:29152043</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3029850User:Steve Klimcak/Sandbox 12019-04-18T20:22:22Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The demethylation of lysine via LSD1 occurs through oxidation via a hydride transfer. Shown in Figure 2 the first step involves the <scene name='81/811710/Fad_highlight/1'>Flavin Adenine Dinucleotide cofactor</scene> initiating a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. In the next step the imine is hydrolyzed and transitions to an hemiaminal. This then breaks down to formaldehyde and the product lysine. <br />
[[Image:LSD1 Mech.jpg|400px|right|thumb|Figure 2]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. The <scene name='81/811712/Hydrophobic_pocket/1'>hydrophobic pocket</scene> shown in green surrounds the FAD in a way such that it exposes the <scene name='81/811710/Fad_n5/4'>catalytic nitrogen(N5)</scene> that is responsible for the two electron demethylation. Another three seperate pockets help bind the histone tail residues to the substrate lysine which is essential for identifying different modifications of the histone tail.<br />
<br />
==Application==<br />
LSD1 plays a pivital role in many biological processes such as cell growth, epithelial-mesenchymal transition, stem cell biology, malignant transformation of cells, and cell differentiation. Malfunctioning of these activities can lead to life threatening diseases such as acute myeloid leukemia and acute lymphoblastic leukemia. Evidence has shown that these activities have ties to prostate and small cell lung cancer so studies have been done to find a reliable inhibitor for LSD1. Monamine oxidases utilize the FAD co-factor much like LSD1 and inhibitors of monamaine oxidase have proven to be successful in inhibiting the activity of LSD1. Thus inhibition of LSD1 opens new pathways for possible treatments for cancers and disorders.<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<ref name="Abdel-Magid">PMID:29152043</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=File:Formula_1.jpg&diff=3026353File:Formula 1.jpg2019-04-12T13:26:49Z<p>Steve Klimcak: </p>
<hr />
<div></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3026268User:Steve Klimcak/Sandbox 12019-04-11T17:39:47Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The methylation of lysine via LSD1 occurs through a 2 electron process. Shown in Figure 3 the first step involves the <scene name='81/811710/Fad_highlight/1'>Flavin Adenine Dinucleotide cofactor</scene> initiating a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. In the next step the imine is hydrolyzed and transitions to an Hemiaminal. This then breaks down easily to formaldehyde and the product lysine. <br />
[[Image:LSD1 Mech.jpg|400px|right|thumb|Figure 3]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. The <scene name='81/811712/Hydrophobic_pocket/1'>hydrophobic pocket</scene> shown in green surrounds the FAD in a way such that it exposes the <scene name='81/811710/Fad_n5/4'>catalytic nitrogen(N5)</scene> that is responsible for the two electron demethylation. Another three seperate pockets help bind the histone tail residues to the substrate lysine which is essential for identifying different modifications of the histone tail.<br />
<br />
==Application==<br />
LSD1 plays a pivital role in many biological processes such as cell growth, epithelial-mesenchymal transition, stem cell biology, malignant transformation of cells, and cell differentiation. Malfunctioning of these activities can lead to life threatening diseases such as acute myeloid leukemia and acute lymphoblastic leukemia. Evidence has shown that these activities have ties to prostate and small cell lung cancer so studies have been done to find a reliable inhibitor for LSD1. Monamine oxidases utilize the FAD co-factor much like LSD1 and inhibitors of monamaine oxidase have proven to be successful in inhibiting the activity of LSD1. Thus inhibition of LSD1 opens new pathways for possible treatments for cancers and disorders.<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<ref name="Abdel-Magid">PMID:29152043</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3023243User:Steve Klimcak/Sandbox 12019-04-09T16:46:43Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The methylation of lysine via LSD1 occurs through a 2 electron process. Shown in Figure 3 the first step involves the <scene name='81/811710/Fad_highlight/1'>Flavin Adenine Dinucleotide cofactor</scene> initiating a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. In the next step the imine is hydrolyzed and transitions to an Hemiaminal. This then breaks down easily to formaldehyde and the product lysine. <br />
[[Image:LSD1 Mech.jpg|400px|right|thumb|Figure 3]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. The <scene name='81/811712/Hydrophobic_pocket/1'>hydrophobic pocket</scene> shown in green surrounds the FAD in a way such that it exposes the <scene name='81/811710/Fad_n5/4'>catalytic nitrogen(N5)</scene> that is responsible for the two electron demethylation. Another three seperate pockets help bind the histone tail residues to the substrate lysine which is essential for identifying different modifications of the histone tail.<br />
<br />
==Application==<br />
<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3023242User:Steve Klimcak/Sandbox 12019-04-09T16:43:16Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The methylation of lysine via LSD1 occurs through a 2 electron process. In the first step the <scene name='81/811710/Fad_highlight/1'>Flavin Adenine Dinucleotide cofactor</scene> initiates a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. In the next step the imine is hydrolyzed and transitions to an Hemiaminal. This then breaks down easily to formaldehyde and the product lysine. <br />
[[Image:LSD1 Mech.jpg|400px|right|thumb|Mechanism]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. The <scene name='81/811712/Hydrophobic_pocket/1'>hydrophobic pocket</scene> shown in green surrounds the FAD in a way such that it exposes the <scene name='81/811710/Fad_n5/4'>catalytic nitrogen(N5)</scene> that is responsible for the two electron demethylation. Another three seperate pockets help bind the histone tail residues to the substrate lysine which is essential for identifying different modifications of the histone tail.<br />
<br />
==Application==<br />
<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3023239User:Steve Klimcak/Sandbox 12019-04-09T16:39:00Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The methylation of lysine via LSD1 occurs through a 2 electron process. In the first step the Flavin Adenine Dinucleotide cofactor initiates a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. In the next step the imine is hydrolyzed and transitions to an Hemiaminal. This then breaks down easily to formaldehyde and the product lysine. <br />
[[Image:LSD1 Mech.jpg|400px|right|thumb|Mechanism]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. The <scene name='81/811712/Hydrophobic_pocket/1'>hydrophobic pocket</scene> shown in green surrounds the FAD in a way such that it exposes the <scene name='81/811710/Fad_n5/4'>catalytic nitrogen(N5)</scene> that is responsible for the two electron demethylation. Another three seperate pockets help bind the histone tail residues to the substrate lysine which is essential for identifying different modifications of the histone tail.<br />
<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3023233User:Steve Klimcak/Sandbox 12019-04-09T16:32:23Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The methylation of lysine via LSD1 occurs through a 2 electron process. In the first step the Flavin Adenine Dinucleotide cofactor initiates a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. In the next step the imine is hydrolyzed and transitions to an Hemiaminal. This then breaks down easily to formaldehyde and the product lysine. <br />
[[Image:LSD1 Mech.jpg|400px|right|thumb|Mechanism]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. The <scene name='81/811712/Hydrophobic_pocket/1'>hydrophobic pocket</scene> shown in green surrounds the FAD in a way such that it exposes the <scene name='81/811710/Fad_n5/4'>catalytic nitrogen(N5)</scene> that is responsible for the two electron demethylation.<br />
<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3023232User:Steve Klimcak/Sandbox 12019-04-09T16:27:18Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The methylation of lysine via LSD1 occurs through a 2 electron process. In the first step the Flavin Adenine Dinucleotide cofactor initiates a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. In the next step the imine is hydrolyzed and transitions to an Hemiaminal. This then breaks down easily to formaldehyde and the product lysine. <br />
[[Image:LSD1 Mech.jpg|400px|right|thumb|Mechanism]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761. The <scene name='81/811712/Hydrophobic_pocket/1'>hydrophobic pocket</scene> shown in green surrounds the <br />
<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3023226User:Steve Klimcak/Sandbox 12019-04-09T16:19:28Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===Mechanism===<br />
The methylation of lysine via LSD1 occurs through a 2 electron process. In the first step the Flavin Adenine Dinucleotide cofactor initiates a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. In the next step the imine is hydrolyzed and transitions to an Hemiaminal. This then breaks down easily to formaldehyde and the product lysine. <br />
[[Image:LSD1 Mech.jpg|400px|right|thumb|Mechanism]]<br />
<br />
===Hydrophobic Pocket===<br />
The hydrophobic pocket located in the active site cavity of LSD1, forms a catalytic chamber where the substrate lysine is oriented and positioned to interact with the <br />
FAD co-factor to initiate demethylation. The specific residues making up the pocket include valine-317, glycine-330, alanine-331, methionine 332, valine-333, phenylalanine-338, leucine-569, asparagine-660, lysine-661, tryptophan 695, serine 749, serine 760, and tyrosine-761.<br />
<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3022691User:Steve Klimcak/Sandbox 12019-04-05T18:21:02Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===mechanism===<br />
The methylation of lysine via LSD1 occurs through a 2 electron process. In the first step the Flavin Adenine Dinucleotide cofactor initiates a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. In the next step the imine is hydrolyzed and transitions to an Hemiaminal. This then breaks down easily to formaldehyde and the product lysine. <br />
[[Image:LSD1 Mech.jpg|400px|right|thumb|Mechanism]]<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3022690User:Steve Klimcak/Sandbox 12019-04-05T18:20:41Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===mechanism===<br />
The methylation of lysine via LSD1 occurs through a 2 electron process. In the first step the Flavin Adenine Dinucleotide cofactor initiates a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. In the next step the imine is hydrolyzed and transitions to an Hemiaminal. This then breaks down easily to formaldehyde and the product lysine. <br />
[[Image:LSD.png|400px|right|thumb|Figure 1 my protein]]<br />
[[Image:LSD1 Mech.jpg|400px|right|thumb|Mechanism]]<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3022689User:Steve Klimcak/Sandbox 12019-04-05T18:20:07Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===mechanism===<br />
The methylation of lysine via LSD1 occurs through a 2 electron process. In the first step the Flavin Adenine Dinucleotide cofactor initiates a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. In the next step the imine is hydrolyzed and transitions to an Hemiaminal. This then breaks down easily to formaldehyde and the product lysine. <br />
[[Image:LSD.png|400px|right|thumb|Figure 1 my protein]]<br />
[[Image:LSD1 Mech.jpg|400px|right|thumb|Mechanism<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=File:LSD1_Mech.jpg&diff=3022685File:LSD1 Mech.jpg2019-04-05T18:16:38Z<p>Steve Klimcak: uploaded a new version of "Image:LSD1 Mech.jpg"</p>
<hr />
<div></div>Steve Klimcakhttps://proteopedia.org/index.php?title=File:LSD1_Mech.jpg&diff=3022684File:LSD1 Mech.jpg2019-04-05T18:15:55Z<p>Steve Klimcak: uploaded a new version of "Image:LSD1 Mech.jpg"</p>
<hr />
<div></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3022672User:Steve Klimcak/Sandbox 12019-04-05T18:03:26Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===mechanism===<br />
The methylation of lysine via LSD1 occurs through a 2 electron process. In the first step the Flavin Adenine Dinucleotide cofactor initiates a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. In the next step the imine is hydrolyzed and transitions to an Hemiaminal. This then breaks down easily to formaldehyde and the product lysine. <br />
[[Image:LSD.png|400px|right|thumb|Figure 1 my protein]]<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3022664User:Steve Klimcak/Sandbox 12019-04-05T17:55:59Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===mechanism===<br />
The methylation of lysine via LSD1 occurs through a 2 electron process. In the first step the Flavin Adenine Dinucleotide cofactor initiates a hydride transfer from the one of the two methyl groups bound to the nitrogen at the lysine tail, via a N5 on the flavin group. An imine cation is then formed at the end of the lysine tail to compensate for the loss of hydride. In the next step the imine is hydrolyzed and <br />
[[Image:LSD.png|400px|right|thumb|Figure 1 my protein]]<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=File:LSD1_Mech.jpg&diff=3019253File:LSD1 Mech.jpg2019-03-29T18:36:20Z<p>Steve Klimcak: </p>
<hr />
<div></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3019245User:Steve Klimcak/Sandbox 12019-03-29T18:16:32Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
<scene name='81/811712/Hydrophobic_pocket/1'>H20phobic Pocket</scene><br />
== Function ==<br />
===mechanism===<br />
[[Image:LSD.png|400px|right|thumb|Figure 1 my protein]]<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3019238User:Steve Klimcak/Sandbox 12019-03-29T17:45:24Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
== Function ==<br />
===mechanism===<br />
[[Image:LSD.png|400px|right|thumb|Figure 1 my protein]]<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3019236User:Steve Klimcak/Sandbox 12019-03-29T17:44:38Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
This is the <scene name='81/811712/Tower_domain/1'>tower domain</scene><br />
===Active Site===<br />
== Function ==<br />
===mechanism===<br />
[[Image:LSD.png|400px|right|thumb|Figure 1 my protein]]<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<references/><br />
<br />
<Structure load='2h94' size='350' frame='true' align='right' caption='LSD1' scene='Structure' /></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3019222User:Steve Klimcak/Sandbox 12019-03-29T17:19:13Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
===Active Site===<br />
== Function ==<br />
===mechanism===<br />
[[Image:LSD.png|400px|right|thumb|Figure 1 my protein]]<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<references/><br />
<br />
<Structure load='2h94' size='350' frame='true' align='right' caption='LSD1' scene='Structure' /></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3019220User:Steve Klimcak/Sandbox 12019-03-29T17:15:54Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
===Active Site===<br />
== Function ==<br />
===mechanism===<br />
[[Image:LSD.png|400px|right|thumb|Figure 1 my protein]]<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<references/><br />
<br />
<Structure load='domains.pse' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /></div>Steve Klimcakhttps://proteopedia.org/index.php?title=File:Domains.pse&diff=3019219File:Domains.pse2019-03-29T17:15:00Z<p>Steve Klimcak: </p>
<hr />
<div></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3016423User:Steve Klimcak/Sandbox 12019-03-22T18:24:08Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
===Active Site===<br />
== Function ==<br />
===mechanism===<br />
[[Image:LSD.png|400px|right|thumb|Figure 1 my protein]]<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref><br />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3016405User:Steve Klimcak/Sandbox 12019-03-22T18:10:59Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
==Structure==<br />
===domains===<br />
===Active Site===<br />
== Function ==<br />
===mechanism===<br />
[[Image:LSD.png|400px|right|thumb|Figure 1 my protein]]<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<references/><br />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3016390User:Steve Klimcak/Sandbox 12019-03-22T18:03:11Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
<br />
== Function ==<br />
[[Image:LSD.png|400px|right|thumb|Figure 1 my protein]]<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<references/><br />
<ref name=”Ransey”>PMID:28504306</ref><br />
<ref name="Khalid">PMID:16275784</ref></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3016388User:Steve Klimcak/Sandbox 12019-03-22T18:01:07Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
<br />
== Function ==<br />
[[Image:LSD.png|400px|right|thumb|Figure 1 my protein]]<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<references/><br />
<ref name=”Ransey”>PMID:28504306</ref></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3016375User:Steve Klimcak/Sandbox 12019-03-22T17:53:32Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
<br />
== Function ==<br />
[[Image:LSD.png|400px|right|thumb|Figure 1 my protein]]<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3016371User:Steve Klimcak/Sandbox 12019-03-22T17:50:38Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
<br />
== Function ==<br />
[[Image:LSD|400px|right|thumb|Figure 1 my protein]].png]]<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3016367User:Steve Klimcak/Sandbox 12019-03-22T17:49:39Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
<br />
== Function ==<br />
[[Image:LSD|400px|right|thumb|Figure Legend]].png]]<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<references/></div>Steve Klimcakhttps://proteopedia.org/index.php?title=User:Steve_Klimcak/Sandbox_1&diff=3016364User:Steve Klimcak/Sandbox 12019-03-22T17:48:52Z<p>Steve Klimcak: </p>
<hr />
<div>= ''LSD Demethylase'' =<br />
<StructureSection load='2h94' size='340' side='right' caption='Caption for this structure' scene=''><br />
This is a default text for your page '''Steve Klimcak/Sandbox 1'''. 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 />
== Introduction ==<br />
<br />
== Function ==<br />
[[Image:LSD|100px|left|thumb|Figure Legend]].png]]<br />
== Disease ==<br />
<br />
== Relevance ==<br />
<br />
== Structural highlights ==<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 />
<references/></div>Steve Klimcak