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1ypo
From Proteopedia
| 1ypo, resolution 3.00Å () | |||||||||
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| Domains: | CLECT_NK_receptors_like | ||||||||
| Related: | 1ypq, 1ypu | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Human Oxidized Low Density Lipoprotein Receptor LOX-1 P3 1 21 Space Group
The lectin-like oxidized low density lipoprotein receptor-1 (Lox-1) mediates the recognition and internalization of oxidatively modified low density lipoprotein by vascular endothelial cells. This interaction results in a number of pro-atherogenic cellular responses that probably play a significant role in the pathology of atherosclerosis. The 1.4 angstrom crystal structure of the extracellular C-type lectin-like domain of human Lox-1 reveals a heart-shaped homodimer with a ridge of six basic amino acids extending diagonally across the apolar top of Lox-1, a central hydrophobic tunnel that extends through the entire molecule, and an electrostatically neutral patch of 12 charged residues that resides next to the tunnel at each opening. Based on the arrangement of critical binding residues on the Lox-1 structure, we propose a binding mode for the recognition of modified low density lipoprotein and other Lox-1 ligands.
The 1.4 angstrom crystal structure of the human oxidized low density lipoprotein receptor lox-1., Park H, Adsit FG, Boyington JC, J Biol Chem. 2005 Apr 8;280(14):13593-9. Epub 2005 Feb 5. PMID:15695803
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1YPO is a 8 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Park H, Adsit FG, Boyington JC. The 1.4 angstrom crystal structure of the human oxidized low density lipoprotein receptor lox-1. J Biol Chem. 2005 Apr 8;280(14):13593-9. Epub 2005 Feb 5. PMID:15695803 doi:10.1074/jbc.M500768200
Page seeded by OCA on Wed Feb 18 01:07:58 2009
