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

Mingyi Chen, Kazuhiko Inoue, Shuh Narumiya, Tomoh Masaki, Tatsuya Sawamura

Research output: Contribution to journalArticle

45 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)215-219
Number of pages5
JournalFEBS Letters
Volume499
Issue number3
DOIs
StatePublished - Jun 22 2001

Keywords

  • C-type lectin
  • Lectin-like oxidized low-density lipoprotein receptor-1
  • Ligand-binding site
  • Oxidized low-density lipoprotein

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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