2HNX

Crystal Structure of aP2

Summary for 2HNX

• Entry DOI: 10.2210/pdb2hnx/pdb
• Descriptor: Fatty acid-binding protein, adipocyte, PHOSPHATE ION, PALMITIC ACID, ... (5 entities in total)
• Functional Keywords: fatty acid binding protein, lipid binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P15090
• Total number of polymer chains: 1
• Total formula weight: 15650.87

Authors

Marr, E.,Tardie, M.,Carty, M.,Brown Phillips, T.,Qiu, X.,Karam, G. (deposition date: 2006-07-13, release date: 2006-11-28, Last modification date: 2024-02-14)

Primary citation

Marr, E.,Tardie, M.,Carty, M.,Brown Phillips, T.,Wang, I.K.,Soeller, W.,Qiu, X.,Karam, G.
Expression, purification, crystallization and structure of human adipocyte lipid-binding protein (aP2).
Acta Crystallogr.,Sect.F, 62:1058-1060, 2006

PubMed 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.

PubMed: 17077479
DOI: 10.1107/S1744309106038656

Experimental method

X-RAY DIFFRACTION (1.5 Å)