Expression, purification, crystallization and structure of human adipocyte lipid-binding protein (aP2).
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.
Marr
Eric
E
Exploratory Medicinal Sciences, Pfizer Global Research and Development Groton Laboratories, Eastern Point Road, Groton, CT 06340, USA.
Tardie
Mark
M
Carty
Maynard
M
Brown Phillips
Tracy
T
Wang
Ing-Kae
IK
Soeller
Walt
W
Qiu
Xiayang
X
Karam
George
G
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
D018076:DNA, Complementary; D050556:Fatty Acid-Binding Proteins