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Title: Purification, crystallization and preliminary X-ray analysis of the ligand-binding domain of human lectin-like oxidized low-density lipoprotein receptor 1 (LOX-1)

Abstract

Two different fragments of the ligand-binding domain of LOX-1, the major receptor for oxidized low-density lipoprotein (LDL) on endothelial cells, have been crystallized in different forms. Two different fragments of the ligand-binding domain of LOX-1, the major receptor for oxidized low-density lipoprotein (LDL) on endothelial cells, have been crystallized in different forms. One crystal form contains the disulfide-linked dimer, which is the form of the molecule present on the cell surface; the other contains a monomeric form of the receptor that lacks the cysteine residue necessary to form disulfide-linked homodimers. The crystal of the monomeric ligand-binding domain belongs to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 56.79, b = 67.57, c = 79.02 Å. The crystal of the dimeric form belongs to space group C2, with unit-cell parameters a = 70.86, b = 49.56, c = 76.73 Å, β = 98.59°. Data for the dimeric form of the LOX-1 ligand-binding domain have been collected to 2.4 Å. For the monomeric form of the ligand-binding domain, native, heavy-atom derivative and SeMet-derivative crystals have been obtained; their diffraction data have been measured to 3.0, 2.4 and 1.8 Å resolution, respectively.

Authors:
; ;  [1];  [2]; ;  [1]
  1. Department of Structural Biology, Biomolecular Engineering Research Institute (BERI), 6-2-3 Furuedai, Suita, Osaka 565-0874 (Japan)
  2. National Food Research Institute, Tsukuba, Ibaraki 305-8642 (Japan)
Publication Date:
OSTI Identifier:
22356007
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F
Additional Journal Information:
Journal Volume: 61; Journal Issue: Pt 5; Other Information: PMCID: PMC1952312; PMID: 16511086; PUBLISHER-ID: ll5018; OAI: oai:pubmedcentral.nih.gov:1952312; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; ATOMS; CRYSTALLIZATION; CRYSTALS; CYSTEINE; DENSITY; DIFFRACTION; DIMERS; LIGANDS; MOLECULES; RECEPTORS; RESOLUTION; SPACE GROUPS; SURFACES

Citation Formats

Ishigaki, Tomoko, Ohki, Izuru, Oyama, Takuji, Machida, Sachiko, Morikawa, Kousuke, and Tate, Shin-ichi. Purification, crystallization and preliminary X-ray analysis of the ligand-binding domain of human lectin-like oxidized low-density lipoprotein receptor 1 (LOX-1). United Kingdom: N. p., 2005. Web. doi:10.1107/S1744309105012042.
Ishigaki, Tomoko, Ohki, Izuru, Oyama, Takuji, Machida, Sachiko, Morikawa, Kousuke, & Tate, Shin-ichi. Purification, crystallization and preliminary X-ray analysis of the ligand-binding domain of human lectin-like oxidized low-density lipoprotein receptor 1 (LOX-1). United Kingdom. https://doi.org/10.1107/S1744309105012042
Ishigaki, Tomoko, Ohki, Izuru, Oyama, Takuji, Machida, Sachiko, Morikawa, Kousuke, and Tate, Shin-ichi. 2005. "Purification, crystallization and preliminary X-ray analysis of the ligand-binding domain of human lectin-like oxidized low-density lipoprotein receptor 1 (LOX-1)". United Kingdom. https://doi.org/10.1107/S1744309105012042.
@article{osti_22356007,
title = {Purification, crystallization and preliminary X-ray analysis of the ligand-binding domain of human lectin-like oxidized low-density lipoprotein receptor 1 (LOX-1)},
author = {Ishigaki, Tomoko and Ohki, Izuru and Oyama, Takuji and Machida, Sachiko and Morikawa, Kousuke and Tate, Shin-ichi},
abstractNote = {Two different fragments of the ligand-binding domain of LOX-1, the major receptor for oxidized low-density lipoprotein (LDL) on endothelial cells, have been crystallized in different forms. Two different fragments of the ligand-binding domain of LOX-1, the major receptor for oxidized low-density lipoprotein (LDL) on endothelial cells, have been crystallized in different forms. One crystal form contains the disulfide-linked dimer, which is the form of the molecule present on the cell surface; the other contains a monomeric form of the receptor that lacks the cysteine residue necessary to form disulfide-linked homodimers. The crystal of the monomeric ligand-binding domain belongs to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 56.79, b = 67.57, c = 79.02 Å. The crystal of the dimeric form belongs to space group C2, with unit-cell parameters a = 70.86, b = 49.56, c = 76.73 Å, β = 98.59°. Data for the dimeric form of the LOX-1 ligand-binding domain have been collected to 2.4 Å. For the monomeric form of the ligand-binding domain, native, heavy-atom derivative and SeMet-derivative crystals have been obtained; their diffraction data have been measured to 3.0, 2.4 and 1.8 Å resolution, respectively.},
doi = {10.1107/S1744309105012042},
url = {https://www.osti.gov/biblio/22356007}, journal = {Acta Crystallographica. Section F},
issn = {1744-3091},
number = Pt 5,
volume = 61,
place = {United Kingdom},
year = {Sun May 01 00:00:00 EDT 2005},
month = {Sun May 01 00:00:00 EDT 2005}
}