Open AccessX‐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(s) -
Zawacka Anna,
Loll Bernhard,
Biesiadka Jacek,
Saenger Wolfram,
UchanskaZiegler Barbara,
Ziegler Andreas
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105037966
Subject(s) - peptide , human leukocyte antigen , hla b , biology , antigen , epitope , peptide sequence , amino acid , microbiology and biotechnology , genetics , biochemistry , gene
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 P 2 1 2 1 2 1 ) and 1.83 Å (self‐peptide pVIPR, RRKWRRWHL; space group P 2 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.