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

Article Details

Citation

Marr E, Tardie M, Carty M, Brown Phillips T, Wang IK, Soeller W, Qiu X, Karam G

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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Nov 1;62(Pt 11):1058-60. Epub 2006 Oct 25.

PubMed ID
17077479 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Fatty acid-binding protein, adipocyteP15090Details