skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: X-ray diffraction analysis of crystals from the human major histocompatibility antigen HLA-B*2706 in complex with a viral peptide and with a self-peptide

Abstract

The crystallization of HLA-B*2706 in complex with two peptides is reported. The human leukocyte antigen (HLA) alleles HLA-B*2704 and HLA-B*2706 show an ethnically restricted distribution and are differentially associated with ankylosing spondylitis, with HLA-B*2706 lacking association with this autoimmune disease. However, the products of the two alleles differ by only two amino acids, at heavy-chain residues 114 (His in HLA-B*2704; Asp in HLA-B*2706) and 116 (Asp in HLA-B*2704; Tyr in HLA-B*2706). Both residues could be involved in contacting amino acids of a bound peptide, suggesting that peptides presented by these subtypes play a role in disease pathogenesis. Two HLA-B*2706–peptide complexes were crystallized using the hanging-drop vapour-diffusion method with PEG as precipitant. Data sets were collected to resolutions of 2.70 Å (viral peptide pLMP2, RRRWRRLTV; space group P2{sub 1}2{sub 1}2{sub 1}) and 1.83 Å (self-peptide pVIPR, RRKWRRWHL; space group P2{sub 1}). Using HLA-B*2705 complexed with the pGR peptide (RRRWHRWRL) as a search model, unambiguous molecular-replacement solutions were found for both HLA-B*2706 complexes.

Authors:
 [1]; ; ;  [2]; ;  [1]
  1. Institut für Immungenetik, Charité - Universitätsmedizin Berlin, Campus Virchow-Klinikum, Humboldt-Universität zu Berlin, Spandauer Damm 130, 14050 Berlin (Germany)
  2. Institut für Chemie und Biochemie/Kristallographie, Freie Universität Berlin, Takustrasse 6, 14195 Berlin (Germany)
Publication Date:
OSTI Identifier:
22356206
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 61; Journal Issue: Pt 12; Other Information: PMCID: PMC1978159; PMID: 16511245; PUBLISHER-ID: en5140; OAI: oai:pubmedcentral.nih.gov:1978159; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; CRYSTALS; DIFFUSION; DISTRIBUTION; MATHEMATICAL SOLUTIONS; RESOLUTION; SOLUTIONS; SPACE GROUPS; X-RAY DIFFRACTION

Citation Formats

Zawacka, Anna, Loll, Bernhard, Biesiadka, Jacek, Saenger, Wolfram, Uchanska-Ziegler, Barbara, and Ziegler, Andreas, E-mail: andreas.ziegler@charite.de. X-ray diffraction analysis of crystals from the human major histocompatibility antigen HLA-B*2706 in complex with a viral peptide and with a self-peptide. United Kingdom: N. p., 2005. Web. doi:10.1107/S1744309105037966.
Zawacka, Anna, Loll, Bernhard, Biesiadka, Jacek, Saenger, Wolfram, Uchanska-Ziegler, Barbara, & Ziegler, Andreas, E-mail: andreas.ziegler@charite.de. X-ray diffraction analysis of crystals from the human major histocompatibility antigen HLA-B*2706 in complex with a viral peptide and with a self-peptide. United Kingdom. doi:10.1107/S1744309105037966.
Zawacka, Anna, Loll, Bernhard, Biesiadka, Jacek, Saenger, Wolfram, Uchanska-Ziegler, Barbara, and Ziegler, Andreas, E-mail: andreas.ziegler@charite.de. Thu . "X-ray diffraction analysis of crystals from the human major histocompatibility antigen HLA-B*2706 in complex with a viral peptide and with a self-peptide". United Kingdom. doi:10.1107/S1744309105037966.
@article{osti_22356206,
title = {X-ray diffraction analysis of crystals from the human major histocompatibility antigen HLA-B*2706 in complex with a viral peptide and with a self-peptide},
author = {Zawacka, Anna and Loll, Bernhard and Biesiadka, Jacek and Saenger, Wolfram and Uchanska-Ziegler, Barbara and Ziegler, Andreas, E-mail: andreas.ziegler@charite.de},
abstractNote = {The crystallization of HLA-B*2706 in complex with two peptides is reported. The human leukocyte antigen (HLA) alleles HLA-B*2704 and HLA-B*2706 show an ethnically restricted distribution and are differentially associated with ankylosing spondylitis, with HLA-B*2706 lacking association with this autoimmune disease. However, the products of the two alleles differ by only two amino acids, at heavy-chain residues 114 (His in HLA-B*2704; Asp in HLA-B*2706) and 116 (Asp in HLA-B*2704; Tyr in HLA-B*2706). Both residues could be involved in contacting amino acids of a bound peptide, suggesting that peptides presented by these subtypes play a role in disease pathogenesis. Two HLA-B*2706–peptide complexes were crystallized using the hanging-drop vapour-diffusion method with PEG as precipitant. Data sets were collected to resolutions of 2.70 Å (viral peptide pLMP2, RRRWRRLTV; space group P2{sub 1}2{sub 1}2{sub 1}) and 1.83 Å (self-peptide pVIPR, RRKWRRWHL; space group P2{sub 1}). Using HLA-B*2705 complexed with the pGR peptide (RRRWHRWRL) as a search model, unambiguous molecular-replacement solutions were found for both HLA-B*2706 complexes.},
doi = {10.1107/S1744309105037966},
journal = {Acta Crystallographica. Section F},
number = Pt 12,
volume = 61,
place = {United Kingdom},
year = {Thu Dec 01 00:00:00 EST 2005},
month = {Thu Dec 01 00:00:00 EST 2005}
}