title: 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.
authors.affiliation: Exploratory Medicinal Sciences, Pfizer Global Research and Development Groton Laboratories, Eastern Point Road, Groton, CT 06340, USA.
authors.forename: Eric
authors.initials: E
authors.lastname: Marr
authors.forename: Mark
authors.initials: M
authors.lastname: Tardie
authors.forename: Maynard
authors.initials: M
authors.lastname: Carty
authors.forename: Tracy
authors.initials: T
authors.lastname: Brown Phillips
authors.forename: Ing-Kae
authors.initials: IK
authors.lastname: Wang
authors.forename: Walt
authors.initials: W
authors.lastname: Soeller
authors.forename: Xiayang
authors.initials: X
authors.lastname: Qiu
authors.forename: George
authors.initials: G
authors.lastname: Karam
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray / Q000379:methods; D018076:DNA, Complementary; D050556:Fatty Acid-Binding Proteins / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D015183:Restriction Mapping
chemical_list: D018076:DNA, Complementary; D050556:Fatty Acid-Binding Proteins