Structural properties of the adipocyte lipid binding protein
Document Type
Article
Publication Title
Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
Abstract
The adipocyte lipid binding protein, ALBP (also adipocyte fatty acid binding protein, A-FABP, 422 protein, aP2, and p15 protein), is one of the most studied of the intracellular lipid binding protein family. Here we sequentially compare the different sources of ALBP and describe the idea that one-third of the amino acid side chains near the N-terminal end appear to play a major role in conformational dynamics and in ligand transfer. Crystallographic data for mouse ALBP are summarized and the ligand binding cavity analyzed in terms of the overall surface and conformational dynamics. The region of the proposed ligand portal is described. Amino acid side chains critical to cavity formation and fatty acid interactions are analyzed by comparing known crystal structures containing a series of different hydrophobic ligands. Finally, we address ALBP ligand binding affinity and thermodynamic studies. Copyright (C) 1999 Elsevier Science B.V.
First Page
106
Last Page
116
DOI
10.1016/S1388-1981(99)00154-7
Publication Date
11-23-1999
Recommended Citation
Reese-Wagoner, Amy; Thompson, James; and Banaszak, Leonard, "Structural properties of the adipocyte lipid binding protein" (1999). Basic Sciences Faculty Publications. 160.
https://doi.org/10.1016/S1388-1981(99)00154-7
https://collections.uhsp.edu/basic-sciences_pubs/160