Proteopedia - User contributions [en]

https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Hong+Phuc+Nguyen Proteopedia - User contributions [en] 2026-10-09T17:41:53Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=Sandbox_Reserved_1549&diff=3037905 Sandbox Reserved 1549 2019-05-05T16:03:02Z

<p>Hong Phuc Nguyen: </p> <hr /> <div><scene name='80/806435/Vlcad/1'>Text To Be Displayed</scene>{{ Sandbox_Reserved_GGC_BHCM4100_1}}<br /> ==A Very Long Chain Acyl-CoA Dehydrogenase==<br /> <StructureSection load='3B96' size='350' frame='true' align='right' caption='Very Long Chain Acyl-CoA Dehydrogenase'/><br /> <br /> == Function ==<br /> <scene name='80/806435/Vlcad/1'>Very long-chain acyl-CoA dehydrogenase</scene> (VLCAD) is one of the five members of acyl-CoA dehydrogenases (ACADs). VLCADs assembles the initial, rate limiting step of mitochondrial fatty acid β-oxidation<ref name="Crystal Structure of human very long-chain VLCAD"/>. The VLCAD has ideal chain length specificity in which fatty acyl-CoA has 16 carbons in length<ref name="Crystal Structure of human very long-chain VLCAD"/>. They are long-, medium-, and short-chain acyl CoA dehydrogenase<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, the activation of acyl CoA dehydrogenase 9 (ACAD-9) is mostly with unsaturated long-chain acyl-CoAs<ref name="Crystal Structure of human very long-chain VLCAD"/>. Unlike other ACADs, mature VLCAD and ACAD-9 are homodimers of 67-kDa subunit which binds to the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. VLCAD and ACAD- 9 possess an additional 180 residues on the C-terminal end, and also with other AVCADs, they possess MCAD-like catalytic glutamate<ref name="Crystal Structure of human very long-chain VLCAD"/>. In fact, not only allows longer chain-length substrates to bind, VLCAD prefers them to bind<ref name="Crystal Structure of human very long-chain VLCAD"/>. C-terminal domain of VLCAD has shown to be subjected for binding to the matrix side of the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. A450P and L462P are human clinical mutants in which located in the C-terminal domain. When these mutants are active and stable, it is reducing the capability to bind the membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. However, there is no clear hydrophobic patch visible that can interact with the membrane, and <scene name='80/806435/Res446/1'>residues 446-478</scene> are the residue that disordered the VLCAD structure<ref name="Crystal Structure of human very long-chain VLCAD"/>. Due to the proximity of <scene name='80/806435/445/1'>residues both 445 and 479 to the surface</scene>, and it expects that the disordered residues occur at the surface of the molecule<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, there are Gln-95 and Glu-99, in which located in MCAD, they help to form the base of the building cavity<ref name="Crystal Structure of human very long-chain VLCAD"/>. In VLCAD, these residues are called glycine (<scene name='80/806435/Gly/1'>Gly-135 and Gly—139</scene>), in which efficiently open up and deepen the binding pocket<ref name="Crystal Structure of human very long-chain VLCAD"/>. <br /> <br /> == Disease ==<br /> VLCDA clinical mutation can lead to a disease state. VLCAD is used to break down very long-chain fatty acids, and they are found in food and body’s fat tissue <ref name="VLCAD deficiency">VLCAD deficiency - Genetics Home Reference https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency</ref>. Fatty acids play a crucial role which provides energy for heart and muscle <ref name="Crystal Structure of human very long-chain VLCAD"/>. Thus, VLCAD deficiency can cause severe neonatal cardiomyopathy and liver failure which occur mostly in adolescence or adulthood <ref name="Crystal Structure of human very long-chain VLCAD">crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2431035/</ref>. In addition, if the body does not have sufficient amount of VLCAD, it would affect the metabolism of the body <ref name="VLCAD deficiency"/>. There are several mutation sites that have been found. Mutation R429W is severe in childhood phenotype <ref name="Crystal Structure of human very long-chain VLCAD"/>. <scene name='80/806435/Helixk/1'>Arg-429</scene> on the helix K makes salt-bridge with <scene name='80/806435/Helixk/1'>Glu-384</scene> on helix I <ref name="Crystal Structure of human very long-chain VLCAD"/>. The enzyme is destabilized, and the salt bridge is broken due to the replacing charged residue with the bulky neutral residue <ref name="Crystal Structure of human very long-chain VLCAD"/>. Another mutation site is R416H which is found on the helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Both sites,<scene name='80/806435/Gln422/1'> R429W and R416H</scene>, are located close to the <scene name='80/806435/Gln422/1'> catalytic glutamate</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Site R416H has <scene name='80/806435/Helixj/1'>Arg-416 interacts with Asp-391</scene> by making salt bridge and interacts <scene name='80/806435/Helixj/1'>Gln-395 </scene> through hydrogen bond <ref name="Crystal Structure of human very long-chain VLCAD"/>. Mutation in R416H causes the problem to the position of helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Furthermore, forming a salt bridge with the opposing monomer can affect the dimer interaction <ref name="Crystal Structure of human very long-chain VLCAD"/>. <br /> <br /> Deficient VLCAD affects 1 person in 40,000 to 120,000 people, thus, it is a very rare diseases <ref name="VLCAD deficiency"/>.<br /> <br /> <br /> == Structural highlights ==<br /> <br /> VLCAD is a mitochondrial inner-membrane-associated protein and is a homodimer of a 71-kDa polypeptide containing 2 mol FAD/mol enzyme <ref name="Souri, M., et al."/>. Both rat and human VLCAD cDNAs encode the entire protein of 655 amino acids, including a 40-amino-acid leader peptide and a 615-amino-acid mature protein <ref name="Souri, M., et al."/>. Three other acyl-CoA dehydrogenases share a high degree of sequence similarity throughout the entire sequences <ref name="Souri, M., et al."/>. VLCAD has a region with a significantly high similarity to other acyl-CoA dehydrogenases at the amino-terminal side, but it has a long tail of approximately 180 amino acid residues at the carboxyl-terminal side, which is not shared with other acyl-CoA dehydrogenases <ref name="Souri, M., et al."/>. Substrate-chain-length specificities of the four acyl-CoA dehydrogenases are different but overlapping <ref name="Souri, M., et al."/>. VLCAD is active toward CoA esters of long-chain and very-long-chain fatty acid <ref name="Souri, M., et al."/>.The overall fold of the N-terminal is about 400 residues of VLCAD is similar to that of the soluble ACADs including medium-chain acyl-CoA dehydrogenase (MCAD) <ref name="Crystal Structure of human very long-chain VLCAD"/>. The novelC-terminal domain forms an -helical bundle that is positioned perpendicular to the two N-terminal helical domains <ref name="Crystal Structure of human very long-chain VLCAD"/>. The fatty acyl moiety of the bound substrate/product is deeply imbedded inside the protein; however, the adenosine pyrophosphate portion of the C14-CoA ligand is disordered because of partial hydrolysis of the thioester bond and high mobility of the CoA moiety <ref name="Crystal Structure of human very long-chain VLCAD"/>.The location of Glu-422with respect to the C2–C3 of the bound ligand and FAD confirms Glu-422 to be the catalytic base <ref name="Crystal Structure of human very long-chain VLCAD"/>. In MCAD, Gln-95 and Glu-99 form the base of the substrate binding cavity <ref name="Crystal Structure of human very long-chain VLCAD"/>. In VLCAD, these residues are glycines (Gly-175 andGly-178), allowing the binding channel to extend for an additional 12 A ˚ and permitting substrate acyl chain lengths as long as 24 carbons <ref name="Crystal Structure of human very long-chain VLCAD"/>.<br /> <br /> == Reference ==<br /> <br /> 1. VLCAD deficiency - Genetics Home Reference - NIH. (2019, April 02). Retrieved April 30, 2019, from https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency<br /> <br /> 2. McAndrew, R. P., Wang, Y., Mohsen, A. W., He, M., Vockley, J., & Kim, J. J. (2008). Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2431035/<br /> <br /> 3. Souri, M., et al. “Relationship between Structure and Substrate-Chain-Length Specificity of Mitochondrial Very-Long-Chain Acyl-Coenzyme A Dehydrogenase.” European Journal Of Biochemistry, vol. 257, no. 3, Nov. 1998, pp. 592–598. EBSCOhost, search.ebscohost.com/login.aspx?direct=true&db=mnh&AN=9839948&site=eds-live&scope=site. from https://http://eds.b.ebscohost.com.libproxyl.ggc.edu/eds/pdfviewer/pdfviewer?vid=2&sid=f09e49a7-ff1c-4d32-b8aa-a3a90cab8b01%40pdc-v-sessmgr06</div>

Hong Phuc Nguyen https://proteopedia.org/index.php?title=Sandbox_Reserved_1549&diff=3037904 Sandbox Reserved 1549 2019-05-05T15:58:30Z

<p>Hong Phuc Nguyen: </p> <hr /> <div>{{ Sandbox_Reserved_GGC_BHCM4100_1}}<br /> ==A Very Long Chain Acyl-CoA Dehydrogenase==<br /> <StructureSection load='3B96' size='350' frame='true' align='right' caption='Very Long Chain Acyl-CoA Dehydrogenase'/><br /> <br /> == Function ==<br /> Very long-chain acyl-CoA dehydrogenase (VLCAD) is one of the five members of acyl-CoA dehydrogenases (ACADs). VLCADs assembles the initial, rate limiting step of mitochondrial fatty acid β-oxidation<ref name="Crystal Structure of human very long-chain VLCAD"/>. The VLCAD has ideal chain length specificity in which fatty acyl-CoA has 16 carbons in length<ref name="Crystal Structure of human very long-chain VLCAD"/>. They are long-, medium-, and short-chain acyl CoA dehydrogenase<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, the activation of acyl CoA dehydrogenase 9 (ACAD-9) is mostly with unsaturated long-chain acyl-CoAs<ref name="Crystal Structure of human very long-chain VLCAD"/>. Unlike other ACADs, mature VLCAD and ACAD-9 are homodimers of 67-kDa subunit which binds to the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. VLCAD and ACAD- 9 possess an additional 180 residues on the C-terminal end, and also with other AVCADs, they possess MCAD-like catalytic glutamate<ref name="Crystal Structure of human very long-chain VLCAD"/>. In fact, not only allows longer chain-length substrates to bind, VLCAD prefers them to bind<ref name="Crystal Structure of human very long-chain VLCAD"/>. C-terminal domain of VLCAD has shown to be subjected for binding to the matrix side of the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. A450P and L462P are human clinical mutants in which located in the C-terminal domain. When these mutants are active and stable, it is reducing the capability to bind the membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. However, there is no clear hydrophobic patch visible that can interact with the membrane, and <scene name='80/806435/Res446/1'>residues 446-478</scene> are the residue that disordered the VLCAD structure<ref name="Crystal Structure of human very long-chain VLCAD"/>. Due to the proximity of <scene name='80/806435/445/1'>residues both 445 and 479 to the surface</scene>, and it expects that the disordered residues occur at the surface of the molecule<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, there are Gln-95 and Glu-99, in which located in MCAD, they help to form the base of the building cavity<ref name="Crystal Structure of human very long-chain VLCAD"/>. In VLCAD, these residues are called glycine (<scene name='80/806435/Gly/1'>Gly-135 and Gly—139</scene>), in which efficiently open up and deepen the binding pocket<ref name="Crystal Structure of human very long-chain VLCAD"/>. <br /> <br /> == Disease ==<br /> VLCDA clinical mutation can lead to a disease state. VLCAD is used to break down very long-chain fatty acids, and they are found in food and body’s fat tissue <ref name="VLCAD deficiency">VLCAD deficiency - Genetics Home Reference https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency</ref>. Fatty acids play a crucial role which provides energy for heart and muscle <ref name="Crystal Structure of human very long-chain VLCAD"/>. Thus, VLCAD deficiency can cause severe neonatal cardiomyopathy and liver failure which occur mostly in adolescence or adulthood <ref name="Crystal Structure of human very long-chain VLCAD">crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2431035/</ref>. In addition, if the body does not have sufficient amount of VLCAD, it would affect the metabolism of the body <ref name="VLCAD deficiency"/>. There are several mutation sites that have been found. Mutation R429W is severe in childhood phenotype <ref name="Crystal Structure of human very long-chain VLCAD"/>. <scene name='80/806435/Helixk/1'>Arg-429</scene> on the helix K makes salt-bridge with <scene name='80/806435/Helixk/1'>Glu-384</scene> on helix I <ref name="Crystal Structure of human very long-chain VLCAD"/>. The enzyme is destabilized, and the salt bridge is broken due to the replacing charged residue with the bulky neutral residue <ref name="Crystal Structure of human very long-chain VLCAD"/>. Another mutation site is R416H which is found on the helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Both sites,<scene name='80/806435/Gln422/1'> R429W and R416H</scene>, are located close to the <scene name='80/806435/Gln422/1'> catalytic glutamate</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Site R416H has <scene name='80/806435/Helixj/1'>Arg-416 interacts with Asp-391</scene> by making salt bridge and interacts <scene name='80/806435/Helixj/1'>Gln-395 </scene> through hydrogen bond <ref name="Crystal Structure of human very long-chain VLCAD"/>. Mutation in R416H causes the problem to the position of helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Furthermore, forming a salt bridge with the opposing monomer can affect the dimer interaction <ref name="Crystal Structure of human very long-chain VLCAD"/>. <br /> <br /> Deficient VLCAD affects 1 person in 40,000 to 120,000 people, thus, it is a very rare diseases <ref name="VLCAD deficiency"/>.<br /> <br /> <br /> == Structural highlights ==<br /> <br /> VLCAD is a mitochondrial inner-membrane-associated protein and is a homodimer of a 71-kDa polypeptide containing 2 mol FAD/mol enzyme <ref name="Souri, M., et al."/>. Both rat and human VLCAD cDNAs encode the entire protein of 655 amino acids, including a 40-amino-acid leader peptide and a 615-amino-acid mature protein <ref name="Souri, M., et al."/>. Three other acyl-CoA dehydrogenases share a high degree of sequence similarity throughout the entire sequences <ref name="Souri, M., et al."/>. VLCAD has a region with a significantly high similarity to other acyl-CoA dehydrogenases at the amino-terminal side, but it has a long tail of approximately 180 amino acid residues at the carboxyl-terminal side, which is not shared with other acyl-CoA dehydrogenases <ref name="Souri, M., et al."/>. Substrate-chain-length specificities of the four acyl-CoA dehydrogenases are different but overlapping <ref name="Souri, M., et al."/>. VLCAD is active toward CoA esters of long-chain and very-long-chain fatty acid <ref name="Souri, M., et al."/>.The overall fold of the N-terminal is about 400 residues of VLCAD is similar to that of the soluble ACADs including medium-chain acyl-CoA dehydrogenase (MCAD) <ref name="Crystal Structure of human very long-chain VLCAD"/>. The novelC-terminal domain forms an -helical bundle that is positioned perpendicular to the two N-terminal helical domains <ref name="Crystal Structure of human very long-chain VLCAD"/>. The fatty acyl moiety of the bound substrate/product is deeply imbedded inside the protein; however, the adenosine pyrophosphate portion of the C14-CoA ligand is disordered because of partial hydrolysis of the thioester bond and high mobility of the CoA moiety <ref name="Crystal Structure of human very long-chain VLCAD"/>.The location of Glu-422with respect to the C2–C3 of the bound ligand and FAD confirms Glu-422 to be the catalytic base <ref name="Crystal Structure of human very long-chain VLCAD"/>. In MCAD, Gln-95 and Glu-99 form the base of the substrate binding cavity <ref name="Crystal Structure of human very long-chain VLCAD"/>. In VLCAD, these residues are glycines (Gly-175 andGly-178), allowing the binding channel to extend for an additional 12 A ˚ and permitting substrate acyl chain lengths as long as 24 carbons <ref name="Crystal Structure of human very long-chain VLCAD"/>.<br /> <br /> == Reference ==<br /> <br /> 1. VLCAD deficiency - Genetics Home Reference - NIH. (2019, April 02). Retrieved April 30, 2019, from https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency<br /> <br /> 2. McAndrew, R. P., Wang, Y., Mohsen, A. W., He, M., Vockley, J., & Kim, J. J. (2008). Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2431035/<br /> <br /> 3. Souri, M., et al. “Relationship between Structure and Substrate-Chain-Length Specificity of Mitochondrial Very-Long-Chain Acyl-Coenzyme A Dehydrogenase.” European Journal Of Biochemistry, vol. 257, no. 3, Nov. 1998, pp. 592–598. EBSCOhost, search.ebscohost.com/login.aspx?direct=true&db=mnh&AN=9839948&site=eds-live&scope=site. from https://http://eds.b.ebscohost.com.libproxyl.ggc.edu/eds/pdfviewer/pdfviewer?vid=2&sid=f09e49a7-ff1c-4d32-b8aa-a3a90cab8b01%40pdc-v-sessmgr06</div>

Hong Phuc Nguyen https://proteopedia.org/index.php?title=Sandbox_Reserved_1549&diff=3037903 Sandbox Reserved 1549 2019-05-05T15:50:47Z

<p>Hong Phuc Nguyen: </p> <hr /> <div>{{ Sandbox_Reserved_GGC_BHCM4100_1}}<br /> ==A Very Long Chain Acyl-CoA Dehydrogenase==<br /> <Structure load='3B96' size='300' frame='true' align='right' caption='' scene='Very Long Chain Acyl-CoA Dehydrogenase'/><br /> <br /> == Function ==<br /> Very long-chain acyl-CoA dehydrogenase (VLCAD) is one of the five members of acyl-CoA dehydrogenases (ACADs). VLCADs assembles the initial, rate limiting step of mitochondrial fatty acid β-oxidation<ref name="Crystal Structure of human very long-chain VLCAD"/>. The VLCAD has ideal chain length specificity in which fatty acyl-CoA has 16 carbons in length<ref name="Crystal Structure of human very long-chain VLCAD"/>. They are long-, medium-, and short-chain acyl CoA dehydrogenase<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, the activation of acyl CoA dehydrogenase 9 (ACAD-9) is mostly with unsaturated long-chain acyl-CoAs<ref name="Crystal Structure of human very long-chain VLCAD"/>. Unlike other ACADs, mature VLCAD and ACAD-9 are homodimers of 67-kDa subunit which binds to the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. VLCAD and ACAD- 9 possess an additional 180 residues on the C-terminal end, and also with other AVCADs, they possess MCAD-like catalytic glutamate<ref name="Crystal Structure of human very long-chain VLCAD"/>. In fact, not only allows longer chain-length substrates to bind, VLCAD prefers them to bind<ref name="Crystal Structure of human very long-chain VLCAD"/>. C-terminal domain of VLCAD has shown to be subjected for binding to the matrix side of the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. A450P and L462P are human clinical mutants in which located in the C-terminal domain. When these mutants are active and stable, it is reducing the capability to bind the membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. However, there is no clear hydrophobic patch visible that can interact with the membrane, and <scene name='80/806435/Res446/1'>residues 446-478</scene> are the residue that disordered the VLCAD structure<ref name="Crystal Structure of human very long-chain VLCAD"/>. Due to the proximity of <scene name='80/806435/445/1'>residues both 445 and 479 to the surface</scene>, and it expects that the disordered residues occur at the surface of the molecule<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, there are Gln-95 and Glu-99, in which located in MCAD, they help to form the base of the building cavity<ref name="Crystal Structure of human very long-chain VLCAD"/>. In VLCAD, these residues are called glycine (<scene name='80/806435/Gly/1'>Gly-135 and Gly—139</scene>), in which efficiently open up and deepen the binding pocket<ref name="Crystal Structure of human very long-chain VLCAD"/>. <br /> <br /> == Disease ==<br /> VLCDA clinical mutation can lead to a disease state. VLCAD is used to break down very long-chain fatty acids, and they are found in food and body’s fat tissue <ref name="VLCAD deficiency">VLCAD deficiency - Genetics Home Reference https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency</ref>. Fatty acids play a crucial role which provides energy for heart and muscle <ref name="Crystal Structure of human very long-chain VLCAD"/>. Thus, VLCAD deficiency can cause severe neonatal cardiomyopathy and liver failure which occur mostly in adolescence or adulthood <ref name="Crystal Structure of human very long-chain VLCAD">crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2431035/</ref>. In addition, if the body does not have sufficient amount of VLCAD, it would affect the metabolism of the body <ref name="VLCAD deficiency"/>. There are several mutation sites that have been found. Mutation R429W is severe in childhood phenotype <ref name="Crystal Structure of human very long-chain VLCAD"/>. <scene name='80/806435/Helixk/1'>Arg-429</scene> on the helix K makes salt-bridge with <scene name='80/806435/Helixk/1'>Glu-384</scene> on helix I <ref name="Crystal Structure of human very long-chain VLCAD"/>. The enzyme is destabilized, and the salt bridge is broken due to the replacing charged residue with the bulky neutral residue <ref name="Crystal Structure of human very long-chain VLCAD"/>. Another mutation site is R416H which is found on the helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Both sites,<scene name='80/806435/Gln422/1'> R429W and R416H</scene>, are located close to the <scene name='80/806435/Gln422/1'> catalytic glutamate</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Site R416H has <scene name='80/806435/Helixj/1'>Arg-416 interacts with Asp-391</scene> by making salt bridge and interacts <scene name='80/806435/Helixj/1'>Gln-395 </scene> through hydrogen bond <ref name="Crystal Structure of human very long-chain VLCAD"/>. Mutation in R416H causes the problem to the position of helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Furthermore, forming a salt bridge with the opposing monomer can affect the dimer interaction <ref name="Crystal Structure of human very long-chain VLCAD"/>. <br /> <br /> Deficient VLCAD affects 1 person in 40,000 to 120,000 people, thus, it is a very rare diseases <ref name="VLCAD deficiency"/>.<br /> <br /> <br /> == Structural highlights ==<br /> <br /> VLCAD is a mitochondrial inner-membrane-associated protein and is a homodimer of a 71-kDa polypeptide containing 2 mol FAD/mol enzyme <ref name="Souri, M., et al."/>. Both rat and human VLCAD cDNAs encode the entire protein of 655 amino acids, including a 40-amino-acid leader peptide and a 615-amino-acid mature protein <ref name="Souri, M., et al."/>. Three other acyl-CoA dehydrogenases share a high degree of sequence similarity throughout the entire sequences <ref name="Souri, M., et al."/>. VLCAD has a region with a significantly high similarity to other acyl-CoA dehydrogenases at the amino-terminal side, but it has a long tail of approximately 180 amino acid residues at the carboxyl-terminal side, which is not shared with other acyl-CoA dehydrogenases <ref name="Souri, M., et al."/>. Substrate-chain-length specificities of the four acyl-CoA dehydrogenases are different but overlapping <ref name="Souri, M., et al."/>. VLCAD is active toward CoA esters of long-chain and very-long-chain fatty acid <ref name="Souri, M., et al."/>.The overall fold of the N-terminal is about 400 residues of VLCAD is similar to that of the soluble ACADs including medium-chain acyl-CoA dehydrogenase (MCAD) <ref name="Crystal Structure of human very long-chain VLCAD"/>. The novelC-terminal domain forms an -helical bundle that is positioned perpendicular to the two N-terminal helical domains <ref name="Crystal Structure of human very long-chain VLCAD"/>. The fatty acyl moiety of the bound substrate/product is deeply imbedded inside the protein; however, the adenosine pyrophosphate portion of the C14-CoA ligand is disordered because of partial hydrolysis of the thioester bond and high mobility of the CoA moiety <ref name="Crystal Structure of human very long-chain VLCAD"/>.The location of Glu-422with respect to the C2–C3 of the bound ligand and FAD confirms Glu-422 to be the catalytic base <ref name="Crystal Structure of human very long-chain VLCAD"/>. In MCAD, Gln-95 and Glu-99 form the base of the substrate binding cavity <ref name="Crystal Structure of human very long-chain VLCAD"/>. In VLCAD, these residues are glycines (Gly-175 andGly-178), allowing the binding channel to extend for an additional 12 A ˚ and permitting substrate acyl chain lengths as long as 24 carbons <ref name="Crystal Structure of human very long-chain VLCAD"/>.<br /> <br /> == Reference ==<br /> <br /> 1. VLCAD deficiency - Genetics Home Reference - NIH. (2019, April 02). Retrieved April 30, 2019, from https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency<br /> <br /> 2. McAndrew, R. P., Wang, Y., Mohsen, A. W., He, M., Vockley, J., & Kim, J. J. (2008). Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2431035/<br /> <br /> 3. Souri, M., et al. “Relationship between Structure and Substrate-Chain-Length Specificity of Mitochondrial Very-Long-Chain Acyl-Coenzyme A Dehydrogenase.” European Journal Of Biochemistry, vol. 257, no. 3, Nov. 1998, pp. 592–598. EBSCOhost, search.ebscohost.com/login.aspx?direct=true&db=mnh&AN=9839948&site=eds-live&scope=site. from https://http://eds.b.ebscohost.com.libproxyl.ggc.edu/eds/pdfviewer/pdfviewer?vid=2&sid=f09e49a7-ff1c-4d32-b8aa-a3a90cab8b01%40pdc-v-sessmgr06</div>

Hong Phuc Nguyen https://proteopedia.org/index.php?title=Sandbox_Reserved_1549&diff=3037456 Sandbox Reserved 1549 2019-05-01T16:32:50Z

<p>Hong Phuc Nguyen: </p> <hr /> <div>{{ Sandbox_Reserved_GGC_BHCM4100_1}}<br /> ==A Very Long Chain Acyl-CoA Dehydrogenase==<br /> <Structure load='3B96' size='300' frame='true' align='right' caption='' scene='Very Long Chain Acyl-CoA Dehydrogenase'/><br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> Very long-chain acyl-CoA dehydrogenase (VLCAD) is one of the five members of acyl-CoA dehydrogenases (ACADs). VLCADs assembles the initial, rate limiting step of mitochondrial fatty acid β-oxidation<ref name="Crystal Structure of human very long-chain VLCAD"/>. The VLCAD has ideal chain length specificity in which fatty acyl-CoA has 16 carbons in length<ref name="Crystal Structure of human very long-chain VLCAD"/>. They are long-, medium-, and short-chain acyl CoA dehydrogenase<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, the activation of acyl CoA dehydrogenase 9 (ACAD-9) is mostly with unsaturated long-chain acyl-CoAs<ref name="Crystal Structure of human very long-chain VLCAD"/>. Unlike other ACADs, mature VLCAD and ACAD-9 are homodimers of 67-kDa subunit which binds to the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. VLCAD and ACAD- 9 possess an additional 180 residues on the C-terminal end, and also with other AVCADs, they possess MCAD-like catalytic glutamate<ref name="Crystal Structure of human very long-chain VLCAD"/>. In fact, not only allows longer chain-length substrates to bind, VLCAD prefers them to bind<ref name="Crystal Structure of human very long-chain VLCAD"/>. C-terminal domain of VLCAD has shown to be subjected for binding to the matrix side of the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. A450P and L462P are human clinical mutants in which located in the C-terminal domain. When these mutants are active and stable, it is reducing the capability to bind the membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. However, there is no clear hydrophobic patch visible that can interact with the membrane, and <scene name='80/806435/Res446/1'>residues 446-478</scene> are the residue that disordered the VLCAD structure<ref name="Crystal Structure of human very long-chain VLCAD"/>. Due to the proximity of <scene name='80/806435/445/1'>residues both 445 and 479 to the surface</scene>, and it expects that the disordered residues occur at the surface of the molecule<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, there are Gln-95 and Glu-99, in which located in MCAD, they help to form the base of the building cavity<ref name="Crystal Structure of human very long-chain VLCAD"/>. In VLCAD, these residues are called glycine (<scene name='80/806435/Gly/1'>Gly-135 and Gly—139</scene>), in which efficiently open up and deepen the binding pocket<ref name="Crystal Structure of human very long-chain VLCAD"/>. <br /> <br /> == Disease ==<br /> VLCDA clinical mutation can lead to a disease state. VLCAD is used to break down very long-chain fatty acids, and they are found in food and body’s fat tissue <ref name="VLCAD deficiency">VLCAD deficiency - Genetics Home Reference https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency</ref>. Fatty acids play a crucial role which provides energy for heart and muscle <ref name="Crystal Structure of human very long-chain VLCAD"/>. Thus, VLCAD deficiency can cause severe neonatal cardiomyopathy and liver failure which occur mostly in adolescence or adulthood <ref name="Crystal Structure of human very long-chain VLCAD">crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2431035/</ref>. In addition, if the body does not have sufficient amount of VLCAD, it would affect the metabolism of the body <ref name="VLCAD deficiency"/>. There are several mutation sites that have been found. Mutation R429W is severe in childhood phenotype <ref name="Crystal Structure of human very long-chain VLCAD"/>. <scene name='80/806435/Helixk/1'>Arg-429</scene> on the helix K makes salt-bridge with <scene name='80/806435/Helixk/1'>Glu-384</scene> on helix I <ref name="Crystal Structure of human very long-chain VLCAD"/>. The enzyme is destabilized, and the salt bridge is broken due to the replacing charged residue with the bulky neutral residue <ref name="Crystal Structure of human very long-chain VLCAD"/>. Another mutation site is R416H which is found on the helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Both sites,<scene name='80/806435/Gln422/1'> R429W and R416H</scene>, are located close to the <scene name='80/806435/Gln422/1'> catalytic glutamate</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Site R416H has <scene name='80/806435/Helixj/1'>Arg-416 interacts with Asp-391 by making salt bridge</scene> and interacts <scene name='80/806435/Helixj/1'>Gln-395 through hydrogen bond</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Mutation in R416H causes the problem to the position of helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Furthermore, forming a salt bridge with the opposing monomer can affect the dimer interaction <ref name="Crystal Structure of human very long-chain VLCAD"/>. <br /> <br /> Deficient VLCAD affects 1 person in 40,000 to 120,000 people, thus, it is a very rare diseases <ref name="VLCAD deficiency"/>.<br /> <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 /> == Notes ==<br /> <references/><br /> <br /> == Reference ==<br /> <br /> 1. VLCAD deficiency - Genetics Home Reference - NIH. (2019, April 02). Retrieved April 30, 2019, from https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency<br /> <br /> 2. McAndrew, R. P., Wang, Y., Mohsen, A. W., He, M., Vockley, J., & Kim, J. J. (2008). Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2431035/</div>

Hong Phuc Nguyen https://proteopedia.org/index.php?title=Sandbox_Reserved_1549&diff=3037455 Sandbox Reserved 1549 2019-05-01T16:23:34Z

<p>Hong Phuc Nguyen: </p> <hr /> <div>{{ Sandbox_Reserved_GGC_BHCM4100_1}}<br /> ==A Very Long Chain Acyl-CoA Dehydrogenase==<br /> <Structure load='3B96' size='300' frame='true' align='right' caption='' scene='Very Long Chain Acyl-CoA Dehydrogenase'/><br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> Very long-chain acyl-CoA dehydrogenase (VLCAD) is one of the five members of acyl-CoA dehydrogenases (ACADs). VLCADs assembles the initial, rate limiting step of mitochondrial fatty acid β-oxidation<ref name="Crystal Structure of human very long-chain VLCAD"/>. The VLCAD has ideal chain length specificity in which fatty acyl-CoA has 16 carbons in length<ref name="Crystal Structure of human very long-chain VLCAD"/>. They are long-, medium-, and short-chain acyl CoA dehydrogenase<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, the activation of acyl CoA dehydrogenase 9 (ACAD-9) is mostly with unsaturated long-chain acyl-CoAs<ref name="Crystal Structure of human very long-chain VLCAD"/>. Unlike other ACADs, mature VLCAD and ACAD-9 are homodimers of 67-kDa subunit which binds to the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. VLCAD and ACAD- 9 possess an additional 180 residues on the C-terminal end, and also with other AVCADs, they possess MCAD-like catalytic glutamate<ref name="Crystal Structure of human very long-chain VLCAD"/>. In fact, not only allows longer chain-length substrates to bind, VLCAD prefers them to bind<ref name="Crystal Structure of human very long-chain VLCAD"/>. C-terminal domain of VLCAD has shown to be subjected for binding to the matrix side of the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. A450P and L462P are human clinical mutants in which located in the C-terminal domain. When these mutants are active and stable, it is reducing the capability to bind the membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. However, there is no clear hydrophobic patch visible that can interact with the membrane, and <scene name='80/806435/Res446/1'>residues 446-478</scene> are the residue that disordered the VLCAD structure<ref name="Crystal Structure of human very long-chain VLCAD"/>. Due to the proximity of residues both 445 and 479 to the surface, and it expects that the disordered residues occur at the surface of the molecule<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, there are Gln-95 and Glu-99, in which located in MCAD, they help to form the base of the building cavity<ref name="Crystal Structure of human very long-chain VLCAD"/>. In VLCAD, these residues are called glycine (<scene name='80/806435/Gly/1'>Gly-135 and Gly—139</scene>), in which efficiently open up and deepen the binding pocket<ref name="Crystal Structure of human very long-chain VLCAD"/>. <br /> <br /> == Disease ==<br /> VLCDA clinical mutation can lead to a disease state. VLCAD is used to break down very long-chain fatty acids, and they are found in food and body’s fat tissue <ref name="VLCAD deficiency">VLCAD deficiency - Genetics Home Reference https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency</ref>. Fatty acids play a crucial role which provides energy for heart and muscle <ref name="Crystal Structure of human very long-chain VLCAD"/>. Thus, VLCAD deficiency can cause severe neonatal cardiomyopathy and liver failure which occur mostly in adolescence or adulthood <ref name="Crystal Structure of human very long-chain VLCAD">crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2431035/</ref>. In addition, if the body does not have sufficient amount of VLCAD, it would affect the metabolism of the body <ref name="VLCAD deficiency"/>. There are several mutation sites that have been found. Mutation R429W is severe in childhood phenotype <ref name="Crystal Structure of human very long-chain VLCAD"/>. <scene name='80/806435/Helixk/1'>Arg-429</scene> on the helix K makes salt-bridge with <scene name='80/806435/Helixk/1'>Glu-384</scene> on helix I <ref name="Crystal Structure of human very long-chain VLCAD"/>. The enzyme is destabilized, and the salt bridge is broken due to the replacing charged residue with the bulky neutral residue <ref name="Crystal Structure of human very long-chain VLCAD"/>. Another mutation site is R416H which is found on the helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Both sites,<scene name='80/806435/Gln422/1'> R429W and R416H</scene>, are located close to the <scene name='80/806435/Gln422/1'> catalytic glutamate</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Site R416H has <scene name='80/806435/Helixj/1'>Arg-416 interacts with Asp-391 by making salt bridge</scene> and interacts <scene name='80/806435/Helixj/1'>Gln-395 through hydrogen bond</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Mutation in R416H causes the problem to the position of helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Furthermore, forming a salt bridge with the opposing monomer can affect the dimer interaction <ref name="Crystal Structure of human very long-chain VLCAD"/>. <br /> <br /> Deficient VLCAD affects 1 person in 40,000 to 120,000 people, thus, it is a very rare diseases <ref name="VLCAD deficiency"/>.<br /> <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 /> == Notes ==<br /> <references/><br /> <br /> == Reference ==<br /> <br /> 1. VLCAD deficiency - Genetics Home Reference - NIH. (2019, April 02). Retrieved April 30, 2019, from https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency<br /> <br /> 2. McAndrew, R. P., Wang, Y., Mohsen, A. W., He, M., Vockley, J., & Kim, J. J. (2008). Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2431035/</div>

Hong Phuc Nguyen https://proteopedia.org/index.php?title=Sandbox_Reserved_1549&diff=3037453 Sandbox Reserved 1549 2019-05-01T16:07:47Z

<p>Hong Phuc Nguyen: </p> <hr /> <div>{{ Sandbox_Reserved_GGC_BHCM4100_1}}<br /> ==A Very Long Chain Acyl-CoA Dehydrogenase==<br /> <Structure load='3B96' size='300' frame='true' align='right' caption='' scene='Very Long Chain Acyl-CoA Dehydrogenase'/><br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> Very long-chain acyl-CoA dehydrogenase (VLCAD) is one of the five members of acyl-CoA dehydrogenases (ACADs). VLCADs assembles the initial, rate limiting step of mitochondrial fatty acid β-oxidation<ref name="Crystal Structure of human very long-chain VLCAD"/>. The VLCAD has ideal chain length specificity in which fatty acyl-CoA has 16 carbons in length<ref name="Crystal Structure of human very long-chain VLCAD"/>. They are long-, medium-, and short-chain acyl CoA dehydrogenase<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, the activation of acyl CoA dehydrogenase 9 (ACAD-9) is mostly with unsaturated long-chain acyl-CoAs<ref name="Crystal Structure of human very long-chain VLCAD"/>. Unlike other ACADs, mature VLCAD and ACAD-9 are homodimers of 67-kDa subunit which binds to the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. VLCAD and ACAD- 9 possess an additional 180 residues on the C-terminal end, and also with other AVCADs, they possess MCAD-like catalytic glutamate<ref name="Crystal Structure of human very long-chain VLCAD"/>. In fact, not only allows longer chain-length substrates to bind, VLCAD prefers them to bind<ref name="Crystal Structure of human very long-chain VLCAD"/>. C-terminal domain of VLCAD has shown to be subjected for binding to the matrix side of the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. A450P and L462P are human clinical mutants in which located in the C-terminal domain. When these mutants are active and stable, it is reducing the capability to bind the membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. However, there is no clear hydrophobic patch visible that can interact with the membrane, and 446-478 are the residue that disordered the VLCAD structure<ref name="Crystal Structure of human very long-chain VLCAD"/>. Due to the proximity of residues both 445 and 479 to the surface, and it expects that the disordered residues occur at the surface of the molecule<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, there are Gln-95 and Glu-99, in which located in MCAD, they help to form the base of the building cavity<ref name="Crystal Structure of human very long-chain VLCAD"/>. In VLCAD, these residues are called glycine (<scene name='80/806435/Gly/1'>Gly-135 and Gly—139</scene>), in which efficiently open up and deepen the binding pocket<ref name="Crystal Structure of human very long-chain VLCAD"/>. <br /> <br /> == Disease ==<br /> VLCDA clinical mutation can lead to a disease state. VLCAD is used to break down very long-chain fatty acids, and they are found in food and body’s fat tissue <ref name="VLCAD deficiency">VLCAD deficiency - Genetics Home Reference https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency</ref>. Fatty acids play a crucial role which provides energy for heart and muscle <ref name="Crystal Structure of human very long-chain VLCAD"/>. Thus, VLCAD deficiency can cause severe neonatal cardiomyopathy and liver failure which occur mostly in adolescence or adulthood <ref name="Crystal Structure of human very long-chain VLCAD">crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2431035/</ref>. In addition, if the body does not have sufficient amount of VLCAD, it would affect the metabolism of the body <ref name="VLCAD deficiency"/>. There are several mutation sites that have been found. Mutation R429W is severe in childhood phenotype <ref name="Crystal Structure of human very long-chain VLCAD"/>. <scene name='80/806435/Helixk/1'>Arg-429</scene> on the helix K makes salt-bridge with <scene name='80/806435/Helixk/1'>Glu-384</scene> on helix I <ref name="Crystal Structure of human very long-chain VLCAD"/>. The enzyme is destabilized, and the salt bridge is broken due to the replacing charged residue with the bulky neutral residue <ref name="Crystal Structure of human very long-chain VLCAD"/>. Another mutation site is R416H which is found on the helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Both sites,<scene name='80/806435/Gln422/1'> R429W and R416H</scene>, are located close to the <scene name='80/806435/Gln422/1'> catalytic glutamate</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Site R416H has <scene name='80/806435/Helixj/1'>Arg-416 interacts with Asp-391 by making salt bridge</scene> and interacts <scene name='80/806435/Helixj/1'>Gln-395 through hydrogen bond</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Mutation in R416H causes the problem to the position of helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Furthermore, forming a salt bridge with the opposing monomer can affect the dimer interaction <ref name="Crystal Structure of human very long-chain VLCAD"/>. <br /> <br /> Deficient VLCAD affects 1 person in 40,000 to 120,000 people, thus, it is a very rare diseases <ref name="VLCAD deficiency"/>.<br /> <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 /> == Notes ==<br /> <references/><br /> <br /> == Reference ==<br /> <br /> 1. VLCAD deficiency - Genetics Home Reference - NIH. (2019, April 02). Retrieved April 30, 2019, from https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency<br /> <br /> 2. McAndrew, R. P., Wang, Y., Mohsen, A. W., He, M., Vockley, J., & Kim, J. J. (2008). Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2431035/</div>

Hong Phuc Nguyen https://proteopedia.org/index.php?title=Sandbox_Reserved_1549&diff=3037441 Sandbox Reserved 1549 2019-05-01T15:37:20Z

<p>Hong Phuc Nguyen: </p> <hr /> <div>{{ Sandbox_Reserved_GGC_BHCM4100_1}}<br /> ==A Very Long Chain Acyl-CoA Dehydrogenase==<br /> <Structure load='3B96' size='300' frame='true' align='right' caption='' scene='Very Long Chain Acyl-CoA Dehydrogenase'/><br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> Very long-chain acyl-CoA dehydrogenase (VLCAD) is one of the five members of acyl-CoA dehydrogenases (ACADs). VLCADs assembles the initial, rate limiting step of mitochondrial fatty acid β-oxidation<ref name="Crystal Structure of human very long-chain VLCAD"/>. The VLCAD has ideal chain length specificity in which fatty acyl-CoA has 16 carbons in length<ref name="Crystal Structure of human very long-chain VLCAD"/>. They are long-, medium-, and short-chain acyl CoA dehydrogenase<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, the activation of acyl CoA dehydrogenase 9 (ACAD-9) is mostly with unsaturated long-chain acyl-CoAs<ref name="Crystal Structure of human very long-chain VLCAD"/>. Unlike other ACADs, mature VLCAD and ACAD-9 are homodimers of 67-kDa subunit which binds to the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. VLCAD and ACAD- 9 possess an additional 180 residues on the C-terminal end, and also with other AVCADs, they possess MCAD-like catalytic glutamate<ref name="Crystal Structure of human very long-chain VLCAD"/>. In fact, not only allows longer chain-length substrates to bind, VLCAD prefers them to bind<ref name="Crystal Structure of human very long-chain VLCAD"/>. C-terminal domain of VLCAD has shown to be subjected for binding to the matrix side of the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. A450P and L462P are human clinical mutants in which located in the C-terminal domain. When these mutants are active and stable, it is reducing the capability to bind the membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. However, there is no clear hydrophobic patch visible that can interact with the membrane, and 446-478 are the residue that disordered the VLCAD structure<ref name="Crystal Structure of human very long-chain VLCAD"/>. Due to the proximity of residues both 445 and 479 to the surface, and it expects that the disordered residues occur at the surface of the molecule<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, there are Gln-95 and Glu-99, in which located in MCAD, they help to form the base of the building cavity<ref name="Crystal Structure of human very long-chain VLCAD"/>. In VLCAD, these residues are called glycine (Gly-135 and Gly—139), in which efficiently open up and deepen the binding pocket<ref name="Crystal Structure of human very long-chain VLCAD"/>. <br /> <br /> == Disease ==<br /> VLCDA clinical mutation can lead to a disease state. VLCAD is used to break down very long-chain fatty acids, and they are found in food and body’s fat tissue <ref name="VLCAD deficiency">VLCAD deficiency - Genetics Home Reference https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency</ref>. Fatty acids play a crucial role which provides energy for heart and muscle <ref name="Crystal Structure of human very long-chain VLCAD"/>. Thus, VLCAD deficiency can cause severe neonatal cardiomyopathy and liver failure which occur mostly in adolescence or adulthood <ref name="Crystal Structure of human very long-chain VLCAD">crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2431035/</ref>. In addition, if the body does not have sufficient amount of VLCAD, it would affect the metabolism of the body <ref name="VLCAD deficiency"/>. There are several mutation sites that have been found. Mutation R429W is severe in childhood phenotype <ref name="Crystal Structure of human very long-chain VLCAD"/>. <scene name='80/806435/Helixk/1'>Arg-429</scene> on the helix K makes salt-bridge with <scene name='80/806435/Helixk/1'>Glu-384</scene> on helix I <ref name="Crystal Structure of human very long-chain VLCAD"/>. The enzyme is destabilized, and the salt bridge is broken due to the replacing charged residue with the bulky neutral residue <ref name="Crystal Structure of human very long-chain VLCAD"/>. Another mutation site is R416H which is found on the helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Both sites,<scene name='80/806435/Gln422/1'> R429W and R416H</scene>, are located close to the <scene name='80/806435/Gln422/1'> catalytic glutamate</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Site R416H has <scene name='80/806435/Helixj/1'>Arg-416 interacts with Asp-391 by making salt bridge</scene> and interacts <scene name='80/806435/Helixj/1'>Gln-395 through hydrogen bond</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Mutation in R416H causes the problem to the position of helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Furthermore, forming a salt bridge with the opposing monomer can affect the dimer interaction <ref name="Crystal Structure of human very long-chain VLCAD"/>. <br /> <br /> Deficient VLCAD affects 1 person in 40,000 to 120,000 people, thus, it is a very rare diseases <ref name="VLCAD deficiency"/>.<br /> <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 /> == Notes ==<br /> <references/><br /> <br /> == Reference ==<br /> <br /> 1. VLCAD deficiency - Genetics Home Reference - NIH. (2019, April 02). Retrieved April 30, 2019, from https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency<br /> <br /> 2. McAndrew, R. P., Wang, Y., Mohsen, A. W., He, M., Vockley, J., & Kim, J. J. (2008). Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2431035/</div>

Hong Phuc Nguyen https://proteopedia.org/index.php?title=Sandbox_Reserved_1549&diff=3037423 Sandbox Reserved 1549 2019-05-01T15:16:55Z

<p>Hong Phuc Nguyen: </p> <hr /> <div>{{ Sandbox_Reserved_GGC_BHCM4100_1}}<br /> ==A Very Long Chain Acyl-CoA Dehydrogenase==<br /> <Structure load='3B96' size='300' frame='true' align='right' caption='' scene='Very Long Chain Acyl-CoA Dehydrogenase' /><br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> Very long-chain acyl-CoA dehydrogenase (VLCAD) is one of the five members of acyl-CoA dehydrogenases (ACADs). VLCADs assembles the initial, rate limiting step of mitochondrial fatty acid β-oxidation<ref name="Crystal Structure of human very long-chain VLCAD"/>. The VLCAD has ideal chain length specificity in which fatty acyl-CoA has 16 carbons in length. They are long-, medium-, and short-chain acyl CoA dehydrogenase<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, the activation of acyl CoA dehydrogenase 9 (ACAD-9) is mostly with unsaturated long-chain acyl-CoAs. Unlike other ACADs, mature VLCAD and ACAD-9 are homodimers of 67-kDa subunit which binds to the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. VLCAD and ACAD- 9 possess an additional 180 residues on the C-terminal end, and also with other AVCADs, they possess MCAD-like catalytic glutamate<ref name="Crystal Structure of human very long-chain VLCAD"/>. In fact, not only allows longer chain-length substrates to bind, VLCAD prefers them to bind<ref name="Crystal Structure of human very long-chain VLCAD"/>. C-terminal domain of VLCAD has shown to be subjected for binding to the matrix side of the inner mitochondrial membrane. A450P and L462P are human clinical mutants in which located in the C-terminal domain. When these mutants are active and stable, it is reducing the capability to bind the membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>.<br /> <br /> == Disease ==<br /> VLCDA clinical mutation can lead to a disease state. VLCAD is used to break down very long-chain fatty acids, and they are found in food and body’s fat tissue <ref name="VLCAD deficiency">VLCAD deficiency - Genetics Home Reference https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency</ref>. Fatty acids play a crucial role which provides energy for heart and muscle <ref name="Crystal Structure of human very long-chain VLCAD"/>. Thus, VLCAD deficiency can cause severe neonatal cardiomyopathy and liver failure which occur mostly in adolescence or adulthood <ref name="Crystal Structure of human very long-chain VLCAD">crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2431035/</ref>. In addition, if the body does not have sufficient amount of VLCAD, it would affect the metabolism of the body <ref name="VLCAD deficiency"/>. There are several mutation sites that have been found. Mutation R429W is severe in childhood phenotype <ref name="Crystal Structure of human very long-chain VLCAD"/>. <scene name='80/806435/Helixk/1'>Arg-429</scene> on the helix K makes salt-bridge with <scene name='80/806435/Helixk/1'>Glu-384</scene> on helix I <ref name="Crystal Structure of human very long-chain VLCAD"/>. The enzyme is destabilized, and the salt bridge is broken due to the replacing charged residue with the bulky neutral residue <ref name="Crystal Structure of human very long-chain VLCAD"/>. Another mutation site is R416H which is found on the helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Both sites,<scene name='80/806435/Gln422/1'> R429W and R416H</scene>, are located close to the <scene name='80/806435/Gln422/1'> catalytic glutamate</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Site R416H has <scene name='80/806435/Helixj/1'>Arg-416 interacts with Asp-391 by making salt bridge</scene> and interacts <scene name='80/806435/Helixj/1'>Gln-395 through hydrogen bond</scene> <ref name="Crystal Structure of human very long-chain VLCAD"/>. Mutation in R416H causes the problem to the position of helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Furthermore, forming a salt bridge with the opposing monomer can affect the dimer interaction <ref name="Crystal Structure of human very long-chain VLCAD"/>. <br /> <br /> Deficient VLCAD affects 1 person in 40,000 to 120,000 people, thus, it is a very rare diseases <ref name="VLCAD deficiency"/>.<br /> <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 /> == Notes ==<br /> <references/><br /> <br /> == Reference ==<br /> <br /> 1. VLCAD deficiency - Genetics Home Reference - NIH. (2019, April 02). Retrieved April 30, 2019, from https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency<br /> <br /> 2. McAndrew, R. P., Wang, Y., Mohsen, A. W., He, M., Vockley, J., & Kim, J. J. (2008). Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2431035/</div>

Hong Phuc Nguyen https://proteopedia.org/index.php?title=Sandbox_Reserved_1549&diff=3034713 Sandbox Reserved 1549 2019-05-01T02:13:38Z

<p>Hong Phuc Nguyen: </p> <hr /> <div>{{ Sandbox_Reserved_GGC_BHCM4100_1}}<br /> ==A Very Long Chain Acyl-CoA Dehydrogenase==<br /> <Structure load='3B96' size='300' frame='true' align='right' caption='' scene='Very Long Chain Acyl-CoA Dehydrogenase' /><br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> Very long-chain acyl-CoA dehydrogenase (VLCAD) is one of the five members of acyl-CoA dehydrogenases (ACADs). VLCADs assembles the initial, rate limiting step of mitochondrial fatty acid β-oxidation<ref name="Crystal Structure of human very long-chain VLCAD"/>. The VLCAD has ideal chain length specificity in which fatty acyl-CoA has 16 carbons in length. They are long-, medium-, and short-chain acyl CoA dehydrogenase<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, the activation of acyl CoA dehydrogenase 9 (ACAD-9) is mostly with unsaturated long-chain acyl-CoAs. Unlike other ACADs, mature VLCAD and ACAD-9 are homodimers of 67-kDa subunit which binds to the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. VLCAD and ACAD- 9 possess an additional 180 residues on the C-terminal end, and also with other AVCADs, they possess MCAD-like catalytic glutamate<ref name="Crystal Structure of human very long-chain VLCAD"/>. In fact, not only allows longer chain-length substrates to bind, VLCAD prefers them to bind<ref name="Crystal Structure of human very long-chain VLCAD"/>. C-terminal domain of VLCAD has shown to be subjected for binding to the matrix side of the inner mitochondrial membrane. A450P and L4462P are human clinical mutants in which located in the C-terminal domain. When these mutants are active and stable, it is reducing the capability to bind the membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>.<br /> <br /> == Disease ==<br /> VLCDA clinical mutation can lead to a disease state. VLCAD is used to break down very long-chain fatty acids, and they are found in food and body’s fat tissue <ref name="VLCAD deficiency">VLCAD deficiency - Genetics Home Reference https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency</ref>. Fatty acids play a crucial role which provides energy for heart and muscle <ref name="Crystal Structure of human very long-chain VLCAD"/>. Thus, VLCAD deficiency can cause severe neonatal cardiomyopathy and liver failure which occur mostly in adolescence or adulthood <ref name="Crystal Structure of human very long-chain VLCAD">crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2431035/</ref>. In addition, if the body does not have sufficient amount of VLCAD, it would affect the metabolism of the body <ref name="VLCAD deficiency"/>. There are several mutation sites that have been found. Mutation R429W is severe in childhood phenotype <ref name="Crystal Structure of human very long-chain VLCAD"/>. Arg-429 on the helix K makes salt-bridge with Glu-384 on helix I <ref name="Crystal Structure of human very long-chain VLCAD"/>. The enzyme is destabilized, and the salt bridge is broken due to the replacing charged residue with the bulky neutral residue <ref name="Crystal Structure of human very long-chain VLCAD"/>. Another mutation site is R416H which is found on the helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Both sites, R429 and R416H, are located close to the catalytic glutamate <ref name="Crystal Structure of human very long-chain VLCAD"/>. Site R416H has Arg-416 interacts with Asp 391 by making salt bridge and interacts with Gln-395 through hydrogen bond <ref name="Crystal Structure of human very long-chain VLCAD"/>. Mutation in R416H causes the problem to the position of helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Furthermore, forming a salt bridge with the opposing monomer can affect the dimer interaction <ref name="Crystal Structure of human very long-chain VLCAD"/>. <br /> <br /> Deficient VLCAD affects 1 person in 40,000 to 120,000 people, thus, it is a very rare diseases <ref name="VLCAD deficiency"/>.<br /> <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 /> == Notes ==<br /> <references/><br /> <br /> == Reference ==<br /> <br /> 1. VLCAD deficiency - Genetics Home Reference - NIH. (2019, April 02). Retrieved April 30, 2019, from https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency<br /> <br /> 2. McAndrew, R. P., Wang, Y., Mohsen, A. W., He, M., Vockley, J., & Kim, J. J. (2008). Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2431035/</div>

Hong Phuc Nguyen https://proteopedia.org/index.php?title=Sandbox_Reserved_1549&diff=3034710 Sandbox Reserved 1549 2019-05-01T02:10:44Z

<p>Hong Phuc Nguyen: </p> <hr /> <div>{{ Sandbox_Reserved_GGC_BHCM4100_1}}<br /> ==A Very Long Chain Acyl-CoA Dehydrogenase==<br /> <Structure load='3B96' size='300' frame='true' align='right' caption='' scene='Very Long Chain Acyl-CoA Dehydrogenase' /><br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> Very long-chain acyl-CoA dehydrogenase (VLCAD) is one of the five members of acyl-CoA dehydrogenases (ACADs). VLCADs assembles the initial, rate limiting step of mitochondrial fatty acid β-oxidation<ref name="Crystal Structure of human very long-chain VLCAD"/>. The VLCAD has ideal chain length specificity in which fatty acyl-CoA has 16 carbons in length. They are long-, medium-, and short-chain acyl CoA dehydrogenase<ref name="Crystal Structure of human very long-chain VLCAD"/>. In addition, the activation of acyl CoA dehydrogenase 9 (ACAD-9) is mostly with unsaturated long-chain acyl-CoAs. Unlike other ACADs, mature VLCAD and ACAD-9 are homodimers of 67-kDa subunit which binds to the inner mitochondrial membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>. VLCAD and ACAD- 9 possess an additional 180 residues on the C-terminal end, and also with other AVCADs, they possess MCAD-like catalytic glutamate<ref name="Crystal Structure of human very long-chain VLCAD"/>. In fact, not only allows longer chain-length substrates to bind, VLCAD prefers them to bind<ref name="Crystal Structure of human very long-chain VLCAD"/>. VLCAD is a monotopic membrane protein, and its C-terminal domain of VLCAD has shown to be subjected for binding to the matrix side of the inner mitochondrial membrane. A450P and L4462P are human clinical mutants in which located in the C-terminal domain. When these mutants are active and stable, it is reducing the capability to bind the membrane<ref name="Crystal Structure of human very long-chain VLCAD"/>.<br /> <br /> == Disease ==<br /> VLCDA clinical mutation can lead to a disease state. VLCAD is used to break down very long-chain fatty acids, and they are found in food and body’s fat tissue <ref name="VLCAD deficiency">VLCAD deficiency - Genetics Home Reference https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency</ref>. Fatty acids play a crucial role which provides energy for heart and muscle <ref name="Crystal Structure of human very long-chain VLCAD"/>. Thus, VLCAD deficiency can cause severe neonatal cardiomyopathy and liver failure which occur mostly in adolescence or adulthood <ref name="Crystal Structure of human very long-chain VLCAD">crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2431035/</ref>. In addition, if the body does not have sufficient amount of VLCAD, it would affect the metabolism of the body <ref name="VLCAD deficiency"/>. There are several mutation sites that have been found. Mutation R429W is severe in childhood phenotype <ref name="Crystal Structure of human very long-chain VLCAD"/>. Arg-429 on the helix K makes salt-bridge with Glu-384 on helix I <ref name="Crystal Structure of human very long-chain VLCAD"/>. The enzyme is destabilized, and the salt bridge is broken due to the replacing charged residue with the bulky neutral residue <ref name="Crystal Structure of human very long-chain VLCAD"/>. Another mutation site is R416H which is found on the helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Both sites, R429 and R416H, are located close to the catalytic glutamate <ref name="Crystal Structure of human very long-chain VLCAD"/>. Site R416H has Arg-416 interacts with Asp 391 by making salt bridge and interacts with Gln-395 through hydrogen bond <ref name="Crystal Structure of human very long-chain VLCAD"/>. Mutation in R416H causes the problem to the position of helix J <ref name="Crystal Structure of human very long-chain VLCAD"/>. Furthermore, forming a salt bridge with the opposing monomer can affect the dimer interaction <ref name="Crystal Structure of human very long-chain VLCAD"/>. <br /> <br /> Deficient VLCAD affects 1 person in 40,000 to 120,000 people, thus, it is a very rare diseases <ref name="VLCAD deficiency"/>.<br /> <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 /> == Notes ==<br /> <references/><br /> <br /> == Reference ==<br /> <br /> 1. VLCAD deficiency - Genetics Home Reference - NIH. (2019, April 02). Retrieved April 30, 2019, from https://ghr.nlm.nih.gov/condition/very-long-chain-acyl-coa-dehydrogenase-deficiency<br /> <br /> 2. McAndrew, R. P., Wang, Y., Mohsen, A. W., He, M., Vockley, J., & Kim, J. J. (2008). Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. The Journal of biological chemistry, 283(14), 9435–9443. doi:10.1074/jbc.M709135200. Retrieved April 30, 2019, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2431035/</div>

Hong Phuc Nguyen https://proteopedia.org/index.php?title=Sandbox_Reserved_1549&diff=3034633 Sandbox Reserved 1549 2019-04-30T14:10:39Z

<p>Hong Phuc Nguyen: </p> <hr /> <div>{{ Sandbox_Reserved_GGC_BHCM4100_1}}<br /> ==A Very Long Chain Acyl-CoA Dehydrogenase==<br /> <Structure load='3B96' size='300' frame='true' align='right' caption='' scene='Very Long Chain Acyl-CoA Dehydrogenase' /><br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> <br /> == Disease ==<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>

Hong Phuc Nguyen https://proteopedia.org/index.php?title=Sandbox_Reserved_1549&diff=3034599 Sandbox Reserved 1549 2019-04-30T00:32:28Z

<p>Hong Phuc Nguyen: </p> <hr /> <div>{{ Sandbox_Reserved_GGC_BHCM4100_1}}<br /> ==A Very Long Chain Acyl-CoA Dehydrogenase==<br /> <Structure load='3B96' size='250' frame='true' align='right' caption='this is my caption' scene='Insert optional scene name here' /><br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> <br /> == Disease ==<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>

Hong Phuc Nguyen https://proteopedia.org/index.php?title=Sandbox_Reserved_1549&diff=3034598 Sandbox Reserved 1549 2019-04-30T00:30:30Z

<p>Hong Phuc Nguyen: </p> <hr /> <div>{{ Sandbox_Reserved_GGC_BHCM4100_1}}<br /> ==A Very Long Chain Acyl-CoA Dehydrogenase==<br /> <Structure load='3B96' size='350' frame='true' align='right' caption='this is my caption' scene='Insert optional scene name here' /><br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> <br /> == Disease ==<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>

Hong Phuc Nguyen https://proteopedia.org/index.php?title=Sandbox_Reserved_1549&diff=3034597 Sandbox Reserved 1549 2019-04-30T00:29:30Z

<p>Hong Phuc Nguyen: </p> <hr /> <div>{{ Sandbox_Reserved_GGC_BHCM4100_1}}<br /> ==A Very Long Chain Acyl-CoA Dehydrogenase==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> <br /> == Disease ==<br /> <br /> == Structural highlights ==<br /> <Structure load='3B96' size='300' frame='true' align='right' caption='this is my caption' scene='Insert optional scene name here' /><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>

Hong Phuc Nguyen https://proteopedia.org/index.php?title=Sandbox_Reserved_1549&diff=3034596 Sandbox Reserved 1549 2019-04-30T00:23:32Z

<p>Hong Phuc Nguyen: </p> <hr /> <div>{{ Sandbox_Reserved_GGC_BHCM4100_1}}<br /> ==A Very Long Chain Acyl-CoA Dehydrogenase==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> <br /> == Disease ==<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>

Hong Phuc Nguyen https://proteopedia.org/index.php?title=Sandbox_Reserved_1549&diff=3030163 Sandbox Reserved 1549 2019-04-22T23:23:45Z

<p>Hong Phuc Nguyen: </p> <hr /> <div>{{ Sandbox_Reserved_GGC_BHCM4100_1}}<br /> ==Your Heading Here (maybe something like 'Structure')==<br /> <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''><br /> This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.<br /> <br /> == Function ==<br /> <br /> == Disease ==<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>

Hong Phuc Nguyen