1YXK

Crystal structure of human lectin-like oxidized low-density lipoprotein receptor 1 (LOX-1) disulfide-linked dimer

Summary for 1YXK

• Entry DOI: 10.2210/pdb1yxk/pdb
• Related: 1YXJ
• Descriptor: oxidised low density lipoprotein (lectin-like) receptor 1 (2 entities in total)
• Functional Keywords: c-type lectin-like domain, lox-1, ctld, scavenger receptor, oxidized ldl receptor, nk cell receptor, lipid binding protein
• 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: 30624.77

Authors

Ohki, I.,Ishigaki, T.,Oyama, T.,Matsunaga, S.,Xie, Q.,Ohnishi-Kameyama, M.,Murata, T.,Tsuchiya, D.,Machida, S.,Morikawa, K.,Tate, S. (deposition date: 2005-02-22, release date: 2005-06-14, Last modification date: 2024-10-23)

Primary citation

Ohki, I.,Ishigaki, T.,Oyama, T.,Matsunaga, S.,Xie, Q.,Ohnishi-Kameyama, M.,Murata, T.,Tsuchiya, D.,Machida, S.,Morikawa, K.,Tate, S.
Crystal structure of human lectin-like, oxidized low-density lipoprotein receptor 1 ligand binding domain and its ligand recognition mode to OxLDL.
Structure, 13:905-917, 2005

PubMed Abstract: 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.

PubMed: 15939022
DOI: 10.1016/j.str.2005.03.016

Experimental method

X-RAY DIFFRACTION (2.4 Å)