Unknown

Dataset Information

0

Expression, purification, crystallization and structure of human adipocyte lipid-binding protein (aP2).


ABSTRACT: 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 A 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.

SUBMITTER: Marr E 

PROVIDER: S-EPMC2225221 | biostudies-literature | 2006 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

Expression, purification, crystallization and structure of human adipocyte lipid-binding protein (aP2).

Marr Eric E   Tardie Mark M   Carty Maynard M   Brown Phillips Tracy T   Wang Ing-Kae IK   Soeller Walt W   Qiu Xiayang X   Karam George G  

Acta crystallographica. Section F, Structural biology and crystallization communications 20061025 Pt 11


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 A 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 exposur  ...[more]

Similar Datasets

| S-EPMC1501108 | biostudies-literature
| S-EPMC4089529 | biostudies-literature
| S-EPMC3702325 | biostudies-literature
| S-EPMC4157427 | biostudies-literature
| S-EPMC2675593 | biostudies-literature
| S-EPMC3755450 | biostudies-literature
| S-EPMC4854568 | biostudies-literature
| S-EPMC3792664 | biostudies-literature
| S-EPMC2150925 | biostudies-literature
| S-EPMC2374255 | biostudies-literature