IFLYSIB 05383
INSTITUTO DE FISICA DE LIQUIDOS Y SISTEMAS BIOLOGICOS
Unidad Ejecutora - UE
artículos
Título:
A hydrophobic loop in Acyl CoA Binding Protein is functionally important for binding to Palmitoyl Coenzyme A. A Molecular Dynamics Study.
Autor/es:
VALLEJO D.F.G.; GRIGERA J.R.; COSTABEL M.
Revista:
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Referencias:
Año: 2007
ISSN:
0141-8130
Resumen:
Acyl CoA Binding Protein (ACBP) plays a key role in lipid metabolism, interacting via apartly unknown mechanism with high affinity with Long Chain Fatty Acyl CoAs (LCFACoAs). At present there is no study of the microscopic way ligand binding is accomplished.We analyzed this process by Molecular Dynamics (MD) simulations. We proposed acomputational model of ligand, able to reproduce some evidence from Nuclear MagneticResonance (NMR) data, quantitative Time Resolved Fluorometry and X-RayCrystallography. We found that a hydrophobic loop, not in the active site, is important forfunction. Besides, multiple sequence alignment shows hydrophobicity (and not the residuesitselves) conservation.
