A hydrophobic loop in acyl-CoA binding protein is functionally important for binding to palmitoyl-coenzyme A: A molecular dynamics study
Acyl-CoA binding protein (ACBP) plays a key role in lipid metabolism, interacting via a partly unknown mechanism with high affinity with long chain fatty acyl-CoAs (LCFA-CoAs). At present there is no study of the microscopic way ligand binding is accomplished. We analyzed this process by molecular d...
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| Veröffentlicht in: | International journal of biological macromolecules 2008-04, Vol.42 (3), p.271-277 |
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| container_title | International journal of biological macromolecules |
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| creator | Vallejo, Diego F.G. Grigera, J. Raúl Costabel, Marcelo D. |
| description | Acyl-CoA binding protein (ACBP) plays a key role in lipid metabolism, interacting via a partly unknown mechanism with high affinity with long chain fatty acyl-CoAs (LCFA-CoAs). At present there is no study of the microscopic way ligand binding is accomplished. We analyzed this process by molecular dynamics (MDs) simulations. We proposed a computational model of ligand, able to reproduce some evidence from nuclear magnetic resonance (NMR) data, quantitative time resolved fluorometry and X-ray crystallography. We found that a hydrophobic loop, not in the active site, is important for function. Besides, multiple sequence alignment shows hydrophobicity (and not the residues itselves) conservation. |
| doi_str_mv | 10.1016/j.ijbiomac.2007.12.003 |
| format | Article |
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Raúl</creatorcontrib><creatorcontrib>Costabel, Marcelo D.</creatorcontrib><title>A hydrophobic loop in acyl-CoA binding protein is functionally important for binding to palmitoyl-coenzyme A: A molecular dynamics study</title><title>International journal of biological macromolecules</title><addtitle>Int J Biol Macromol</addtitle><description>Acyl-CoA binding protein (ACBP) plays a key role in lipid metabolism, interacting via a partly unknown mechanism with high affinity with long chain fatty acyl-CoAs (LCFA-CoAs). At present there is no study of the microscopic way ligand binding is accomplished. We analyzed this process by molecular dynamics (MDs) simulations. We proposed a computational model of ligand, able to reproduce some evidence from nuclear magnetic resonance (NMR) data, quantitative time resolved fluorometry and X-ray crystallography. We found that a hydrophobic loop, not in the active site, is important for function. Besides, multiple sequence alignment shows hydrophobicity (and not the residues itselves) conservation.</description><subject>Acyl-coenzyme A binding protein</subject><subject>Computer Simulation</subject><subject>Crystallography, X-Ray</subject><subject>Diazepam Binding Inhibitor - chemistry</subject><subject>Diazepam Binding Inhibitor - metabolism</subject><subject>Humans</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Hydrophobic interaction</subject><subject>Ligands</subject><subject>Lipid Metabolism - physiology</subject><subject>Lipid protein interactions</subject><subject>Long chain fatty acyl-coenzyme A</subject><subject>Models, Molecular</subject><subject>Molecular dynamics</subject><subject>Nuclear Magnetic Resonance, Biomolecular</subject><subject>Palmitoyl Coenzyme A - chemistry</subject><subject>Palmitoyl Coenzyme A - metabolism</subject><subject>Protein Binding - physiology</subject><issn>0141-8130</issn><issn>1879-0003</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhq0K1G4Lf6HyiVtSf2zihBPRqnxIlbjA2XLsSeuVY6e2gxR-AT8bV7vAkdOMZp6ZVzMvQreU1JTQ9u5Y2-Now6x0zQgRNWU1IfwC7Wgn-oqU_BXaEbqnVUc5uULXKR1LtW1od4muaMf2rO26Hfo14KfNxLA8hdFq7EJYsPVY6c1VhzDg0Xpj_SNeYshQGjbhafU62-CVcxu28xJiVj7jKcS_dA54UW62OZQ1OoD_uc2Ah_d4wHNwoFenIjabV7PVCae8mu0Nej0pl-DtOd6g7x_vvx0-Vw9fP305DA-V5m2bq54DN43Q417AZPYTazjVwCZCWNMR1o9Tz-nIFFFaGRCdZpr3DRfCMEpFI_gNenfaWy56XiFlOdukwTnlIaxJCsI5ZYwUsD2BOoaUIkxyiXZWcZOUyBcP5FH-8UC-eCApk-XvZfD2rLCOM5h_Y-enF-DDCYBy5w8LUSZtwWswNoLO0gT7P43fpMOdng</recordid><startdate>20080401</startdate><enddate>20080401</enddate><creator>Vallejo, Diego F.G.</creator><creator>Grigera, J. 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Raúl</creatorcontrib><creatorcontrib>Costabel, Marcelo D.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>International journal of biological macromolecules</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vallejo, Diego F.G.</au><au>Grigera, J. 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| fulltext | fulltext |
| identifier | ISSN: 0141-8130 |
| ispartof | International journal of biological macromolecules, 2008-04, Vol.42 (3), p.271-277 |
| issn | 0141-8130 1879-0003 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Acyl-coenzyme A binding protein Computer Simulation Crystallography, X-Ray Diazepam Binding Inhibitor - chemistry Diazepam Binding Inhibitor - metabolism Humans Hydrophobic and Hydrophilic Interactions Hydrophobic interaction Ligands Lipid Metabolism - physiology Lipid protein interactions Long chain fatty acyl-coenzyme A Models, Molecular Molecular dynamics Nuclear Magnetic Resonance, Biomolecular Palmitoyl Coenzyme A - chemistry Palmitoyl Coenzyme A - metabolism Protein Binding - physiology |
| title | A hydrophobic loop in acyl-CoA binding protein is functionally important for binding to palmitoyl-coenzyme A: A molecular dynamics study |
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