Open AccessExpression, purification, crystallization and structure of human adipocyte lipid‐binding protein (aP2)
Author(s) -
Marr Eric,
Tardie Mark,
Carty Maynard,
Brown Phillips Tracy,
Wang IngKae,
Soeller Walt,
Qiu Xiayang,
Karam George
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106038656
Subject(s) - fatty acid binding protein , chemistry , intracellular , biochemistry , plasma protein binding , crystallization , binding site , adipocyte , ligand (biochemistry) , binding protein , protein structure , biophysics , microbiology and biotechnology , biology , receptor , adipose tissue , gene , organic chemistry
Human adipocyte lipid‐binding protein (aP2) belongs to a family of intracellular lipid‐binding proteins involved in the transport and storage of lipids. Here, the crystal structure of human aP2 with a bound palmitate is described at 1.5 Å resolution. Unlike the known crystal structure of murine aP2 in complex with palmitate, this structure shows that the fatty acid is in a folded conformation and that the loop containing Phe57 acts as a lid to regulate ligand binding by excluding solvent exposure to the central binding cavity.