1YPQ
Human Oxidized Low Density Lipoprotein Receptor LOX-1 Dioxane Complex
Summary for 1YPQ
Entry DOI | 10.2210/pdb1ypq/pdb |
Related | 1YPO 1YPU |
Descriptor | oxidised low density lipoprotein (lectin-like) receptor 1, 1,4-DIETHYLENE DIOXIDE (3 entities in total) |
Functional Keywords | oxidized low density lipoprotein receptor, lox-1, ctld, c-type lectin like domain, nk cell receptor, immune system |
Biological source | Homo sapiens (human) |
Cellular location | Cell membrane; Single-pass type II membrane protein: P78380 |
Total number of polymer chains | 2 |
Total formula weight | 30712.87 |
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 citation | Park, 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: 15695803DOI: 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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