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Crystal structure of axolotl ( Ambystoma mexicanum ) liver bile acid‐binding protein bound to cholic and oleic acid
Author(s) -
Capaldi Stefano,
Guariento Mara,
Perduca Massimiliano,
Di Pietro Santiago M.,
Santomé José A.,
Monaco Hugo L.
Publication year - 2006
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.20961
Subject(s) - oleic acid , fatty acid binding protein , ligand (biochemistry) , cholic acid , axolotl , binding protein , biochemistry , ambystoma mexicanum , bile acid , chemistry , molecule , binding site , biology , crystallography , stereochemistry , receptor , gene , genetics , regeneration (biology) , organic chemistry
The family of the liver bile acid‐binding proteins (L‐BABPs), formerly called liver basic fatty acid‐binding proteins (Lb‐FABPs) shares fold and sequence similarity with the paralogous liver fatty acid‐binding proteins (L‐FABPs) but has a different stoichiometry and specificity of ligand binding. This article describes the first X‐ray structure of a member of the L‐BABP family, axolotl ( Ambystoma mexicanum ) L‐BABP, bound to two different ligands: cholic and oleic acid. The protein binds one molecule of oleic acid in a position that is significantly different from that of either of the two molecules that bind to rat liver FABP. The stoichiometry of binding of cholate is of two ligands per protein molecule, as observed in chicken L‐BABP. The cholate molecule that binds buried most deeply into the internal cavity overlaps well with the analogous bound to chicken L‐BABP, whereas the second molecule, which interacts with the first only through hydrophobic contacts, is more external and exposed to the solvent. Proteins 2006. © 2006 Wiley‐Liss, Inc.