Abstract
The liver bile acid‐binding proteins, L‐BABPs, formerly called the liver “basic” fatty acid‐binding proteins, are a subfamily of the fatty acid‐binding proteins, FABPs. All the members of this protein group share the same fold: a 10 stranded β barrel in which two short helices are inserted in between the first and the second strand of antiparallel β sheet. The barrel encloses the ligand binding cavity of the protein while the two helices are believed to be involved in ligand accessibility to the binding site. The L‐BABP subfamily has been found to be present in the liver of several vertebrates: fish, amphibians, reptiles, and birds but not in mammals. The members of the FABP family present in mammals that appear to be more closely related to the L‐BABPs are the liver FABPs and the ileal BABPs, both very extensively studied. Several L‐BABP X‐ray structures are available and chicken L‐BABP has also been studied using NMR spectroscopy. The stoichiometry of ligand binding for bile acids, first determined by X‐ray crystallography for the chicken liver protein, is of two cholates per protein molecule with the only exception of zebrafish L‐BABP which, due to the presence of a disulfide bridge, has a stoichiometry of 1:1. The stoichiometry of ligand binding for fatty acids, determined with several different techniques, is 1:1. An unanswered question of great relevance is the identity of the protein that in mammals performs the function that in other vertebrates is carried out by the L‐BABPS. © 2009 Wiley Periodicals, Inc. Biopolymers 91: 1196–1202, 2009.
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