Expression, purification, crystallization and structure of human adipocyte lipid-binding protein (aP2)
Journal Article
·
· Acta Crystallographica. Section F
- Exploratory Medicinal Sciences, Pfizer Global Research and Development Groton Laboratories, Eastern Point Road, Groton, CT 06340 (United States)
- Research Technology Center, Pfizer Global Research and Development Laboratories, Cambridge, MA (United States)
- Cardiovascular and Metabolic Diseases, Pfizer Global Research and Development Groton Laboratories, Eastern Point Road, Groton, CT 06340 (United States)
The crystal structure of human adipocyte lipid-binding protein (aP2) with a bound palmitate is reported at 1.5 Å resolution. 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 Å 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.
- OSTI ID:
- 22356398
- Journal Information:
- Acta Crystallographica. Section F, Vol. 62, Issue Pt 11; Other Information: PMCID: PMC2225221; PMID: 17077479; PUBLISHER-ID: ll5083; OAI: oai:pubmedcentral.nih.gov:2225221; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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