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1YPQ

Human Oxidized Low Density Lipoprotein Receptor LOX-1 Dioxane Complex

Summary for 1YPQ
Entry DOI10.2210/pdb1ypq/pdb
Related1YPO 1YPU
Descriptoroxidised low density lipoprotein (lectin-like) receptor 1, 1,4-DIETHYLENE DIOXIDE (3 entities in total)
Functional Keywordsoxidized low density lipoprotein receptor, lox-1, ctld, c-type lectin like domain, nk cell receptor, immune system
Biological sourceHomo sapiens (human)
Cellular locationCell membrane; Single-pass type II membrane protein: P78380
Total number of polymer chains2
Total formula weight30712.87
Authors
Park, H.,Adsit, F.G.,Boyington, J.C. (deposition date: 2005-01-31, release date: 2005-02-08, Last modification date: 2024-11-06)
Primary citationPark, H.,Adsit, F.G.,Boyington, J.C.
The 1.4 angstrom crystal structure of the human oxidized low density lipoprotein receptor lox-1.
J.Biol.Chem., 280:13593-13599, 2005
Cited by
PubMed Abstract: 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.
PubMed: 15695803
DOI: 10.1074/jbc.M500768200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.4 Å)
Structure validation

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