1YXJ

Crystal structure of human lectin-like oxidized low-density lipoprotein receptor 1 (LOX-1) at low pH

1YXJ の概要

• エントリーDOI: 10.2210/pdb1yxj/pdb
• 関連するPDBエントリー: 1YXK
• 分子名称: oxidised low density lipoprotein (lectin-like) receptor 1, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: c-type lectin-like domain, lox-1, ctld, scavenger receptor, oxidized ldl receptor, nk cell receptor, lipid binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane; Single-pass type II membrane protein: P78380
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30201.44

構造登録者

Ohki, I.,Ishigaki, T.,Oyama, T.,Matsunaga, S.,Xie, Q.,Ohnishi-Kameyama, M.,Murata, T.,Tsuchiya, D.,Machida, S.,Morikawa, K.,Tate, S. (登録日: 2005-02-22, 公開日: 2005-06-14, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.78 Å)