Preliminary X‐ray diffraction analysis of crystals from the recombinantly expressed human major histocompatibility antigen HLA‐B*2704 in complex with a viral peptide and with a self‐peptide

Publisher： John Wiley & Sons Inc

E-ISSN： 1744-3091|61|10|939-941

ISSN： 1744-3091

Source： Acta Crystallographica Section F, Vol.61, Iss.10, 2005-10, pp. : 939-941

Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.

Previous Menu Next

Abstract

The product of the human leukocyte antigen (HLA) gene HLA‐B*2704 differs from that of the prototypical subtype HLA‐B*2705 by three amino acids at heavy‐chain residues 77 (Ser instead of Asp), 152 (Glu instead of Val) and 211 (Gly instead of Ala). In contrast to the ubiquitous HLA‐B*2705 subtype, HLA‐B*2704 occurs only in orientals. Both subtypes are strongly associated with spondyloarthropathies and the peptides presented by these subtypes are suspected to play a role in disease pathogenesis. HLA‐B*2704 was crystallized in complex with a viral peptide and with a self‐peptide using the hanging‐drop vapour‐diffusion method with PEG as a precipitant. Both crystals belong to space group P2₁2₁2₁. Data sets were collected to 1.60 Å (complex with the self‐peptide pVIPR) or to 1.90 Å (complex with the viral peptide pLMP2) resolution using synchrotron radiation. With HLA‐B*2705 complexed with pVIPR as a search model, unambiguous molecular‐replacement solutions were found for the complexes of HLA‐B*2704 with both peptides.