1YXJ: Crystal Structure Of Human Lectin-like Oxidized Low-density Lipoprotein Receptor 1 (lox-1) At Low Ph

Lectin-like, oxidized low-density lipoprotein (LDL) receptor 1, LOX-1, is the major receptor for oxidized LDL (OxLDL) in endothelial cells. We have determined the crystal structure of the ligand binding domain of LOX-1, with a short stalk region connecting the domain to the membrane-spanning region, as a homodimer linked by an interchain disulfide bond. In vivo assays with LOX-1 mutants revealed that the "basic spine," consisting of linearly aligned arginine residues spanning over the dimer surface, is responsible for ligand binding. Single amino acid substitution in the dimer interface caused a severe reduction in LOX-1 binding activity, suggesting that the correct dimer arrangement is crucial for binding to OxLDL. Based on the LDL model structure, possible binding modes of LOX-1 to OxLDL are proposed.
PDB ID: 1YXJDownload
MMDB ID: 33773
PDB Deposition Date: 2005/2/22
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 1.78  Å
Source Organism:
Similar Structures:
Biological Unit for 1YXJ: dimeric; determined by author
Molecular Components in 1YXJ
Label Count Molecule
Proteins (2 molecules)
Oxidised LOW Density Lipoprotein (Lectin-like) Receptor 1(Gene symbol: OLR1)
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

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