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 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.
Vallejo
Diego F G
DF
Instituto de Física de Líquidos y Sistemas Biológicos (IFLYSIB), UNLP-CONICET-CIC, Argentina.
Grigera
J Raúl
JR
Costabel
Marcelo D
MD
D003198:Computer Simulation; D018360:Crystallography, X-Ray; D026261:Diazepam Binding Inhibitor / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008024:Ligands; D050356:Lipid Metabolism / Q000502:physiology; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010171:Palmitoyl Coenzyme A / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding / Q000502:physiology
D026261:Diazepam Binding Inhibitor; D008024:Ligands; D010171:Palmitoyl Coenzyme A