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Merck

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

Acta crystallographica. Section F, Structural biology and crystallization communications (2006-11-02)
Eric Marr, Mark Tardie, Maynard Carty, Tracy Brown Phillips, Ing-Kae Wang, Walt Soeller, Xiayang Qiu, George Karam
ABSTRAKT

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.