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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

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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]

PMID: 17077479

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