| Literature DB >> 17077479 |
Eric Marr1, Mark Tardie, Maynard Carty, Tracy Brown Phillips, Ing-Kae Wang, Walt Soeller, Xiayang Qiu, George Karam.
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.Entities:
Mesh:
Substances:
Year: 2006 PMID: 17077479 PMCID: PMC2225221 DOI: 10.1107/S1744309106038656
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091