Liver fatty acid binding protein: Species variation and the accommodation of different ligands
Document Type
Article
Publication Title
Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
Abstract
The crystal structure of rat liver fatty acid binding protein (LFABP) and an alignment of amino acid sequences of all known species have been used to demonstrate two groups or sub-classes. Based on estimates at neutral pH and the electrostatic field calculated using the crystal coordinates, some evidence of changes that occur in going from holo- to apo-forms has been obtained. LFABP belongs to a large family frequently referred to as the intracellular lipid binding proteins or iLBPs. LFABP, unlike other family members, has two fatty acid binding sites. The two cavity sites have been reviewed and arguments for interactions between the sites are presented. Based on the crystal structure of rat LFABP, differences between the A and B groups have been postulated. Last of all, hypothetical models have been built of complexes of LFABP and heme, and LFABP and oleoyl CoA. In both cases, the stoichiometry is one to one and the models show why this is likely. Copyright (C) 1999 Elsevier Science B.V.
First Page
117
Last Page
130
DOI
10.1016/S1388-1981(99)00146-8
Publication Date
11-23-1999
Recommended Citation
Thompson, James; Reese-Wagoner, Amy; and Banaszak, Leonard, "Liver fatty acid binding protein: Species variation and the accommodation of different ligands" (1999). Basic Sciences Faculty Publications. 161.
https://doi.org/10.1016/S1388-1981(99)00146-8
https://collections.uhsp.edu/basic-sciences_pubs/161