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

Publisher： John Wiley & Sons Inc

E-ISSN： 1744-3091|61|12|1097-1099

ISSN： 1744-3091

Source： Acta Crystallographica Section F, Vol.61, Iss.12, 2005-12, pp. : 1097-1099

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Abstract

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 P2₁2₁2₁) and 1.83 Å (self‐peptide pVIPR, RRKWRRWHL; space group P2₁). 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.