Ontology highlight
ABSTRACT:
SUBMITTER: Marr E
PROVIDER: S-EPMC2225221 | biostudies-literature | 2006 Nov
REPOSITORIES: biostudies-literature
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]