Requirements of basic amino acid residues within the lectin‐like domain of LOX‐1 for the binding of oxidized low‐density lipoprotein

FEBS Letters

Chen, Mingyi²  Sawamura, Tatsuya²  Masaki, Tomoh²  Narumiya, Shuh¹  Inoue, Kazuhiko² 

[1] Department of Pharmacology, Faculty of Medicine, Kyoto University, Kyoto 606, Japan;National Cardiovascular Center Research Institute, Suita, Osaka 565-8565, Japan

关键词: Oxidized low-density lipoprotein;    Lectin-like oxidized low-density lipoprotein receptor-1;    C-type lectin;    Ligand-binding site;   

DOI  :  10.1016/S0014-5793(01)02557-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Lectin-like OxLDL receptor-1 (LOX-1) was identified as the major receptor for oxidized low-density lipoprotein (OxLDL) in aortic endothelial cells. LOX-1 is a type II membrane protein that structurally belongs to the C-type lectin family. Here, we found that the lectin-like domain of LOX-1 is essential for ligand binding, but the neck domain is not. In particular, the large loop between the third and fourth cysteine of the lectin-like domain plays a critical role for OxLDL binding as well as C-terminal end residues. Alanine-directed mutagenesis of the basic amino acid residues around this region revealed that all of the basic residues are involved in OxLDL binding. Simultaneous mutations of these basic residues almost abolished the OxLDL-binding activity of LOX-1. Electrostatic interaction between basic residues in the lectin-like domain of LOX-1 and negatively charged OxLDL is critical for the binding activity of LOX-1.

【 授权许可】

Unknown