1yxk

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Revision as of 18:19, 12 November 2007

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spinqualitylabelsall models 1yxk, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

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.

Disease

Known disease associated with this structure: Myocardial infarction, susceptibility to OMIM:[602601]

About this Structure

1YXK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human lectin-like, oxidized low-density lipoprotein receptor 1 ligand binding domain and its ligand recognition mode to OxLDL., Ohki I, Ishigaki T, Oyama T, Matsunaga S, Xie Q, Ohnishi-Kameyama M, Murata T, Tsuchiya D, Machida S, Morikawa K, Tate S, Structure. 2005 Jun;13(6):905-17. PMID:15939022

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