TY - JOUR
T1 - Structural properties of the adipocyte lipid binding protein
AU - Reese-Wagoner, Amy
AU - Thompson, James
AU - Banaszak, Leonard
N1 - Funding Information:
The authors are grateful to members of the Banaszak, Ohlendorf, and Bernlohr laboratories at the University of Minnesota for many helpful discussions and collaborations. We also thank Dr. Jeramia Ory, presently at Washington University, for his insightful help. As part of the long-range studies of the ALBPs, we acknowledge continuing support from the NIH (GM13925) and the Minnesota Supercomputer Institute.
PY - 1999/11/23
Y1 - 1999/11/23
N2 - 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.
AB - 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.
KW - Adipocyte
KW - Fatty acid binding protein
KW - Intracellular lipid binding protein
KW - β-Barrel protein
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U2 - 10.1016/S1388-1981(99)00154-7
DO - 10.1016/S1388-1981(99)00154-7
M3 - Review article
C2 - 10570239
AN - SCOPUS:0032751680
SN - 1388-1981
VL - 1441
SP - 106
EP - 116
JO - Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
JF - Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
IS - 2-3
ER -