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2hnx
From Proteopedia
| 2hnx, resolution 1.50Å () | |||||||||
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| Ligands: | , , | ||||||||
| Gene: | FABP4 (Homo sapiens) | ||||||||
| Domains: | Lipocalin | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Crystal Structure of 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.
Expression, purification, crystallization and structure of human adipocyte lipid-binding protein (aP2)., Marr E, Tardie M, Carty M, Brown Phillips T, Wang IK, Soeller W, Qiu X, Karam G, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Nov 1;62(Pt, 11):1058-60. Epub 2006 Oct 25. PMID:17077479
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
2HNX is a 1 chain structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Marr E, Tardie M, Carty M, Brown Phillips T, Wang IK, Soeller W, Qiu X, Karam G. Expression, purification, crystallization and structure of human adipocyte lipid-binding protein (aP2). Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Nov 1;62(Pt, 11):1058-60. Epub 2006 Oct 25. PMID:17077479 doi:10.1107/S1744309106038656
Page seeded by OCA on Mon Feb 16 16:08:12 2009
