Purification, crystallization and preliminary X‐ray diffraction analysis of the human major histocompatibility antigen HLA‐B*2703 complexed with a viral peptide and with a self‐peptide

Publisher： John Wiley & Sons Inc

E-ISSN： 1744-3091|61|4|372-374

ISSN： 1744-3091

Source： Acta Crystallographica Section F, Vol.61, Iss.4, 2005-04, pp. : 372-374

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Abstract

The product of the human leukocyte antigen (HLA) gene HLA‐B*2703 differs from that of the prototypical subtype HLA‐B*2705 by a single amino acid at heavy‐chain residue 59 that is involved in anchoring the peptide N‐terminus within the A pocket of the molecule. Two B*2703–peptide complexes were crystallized using the hanging‐drop vapour‐diffusion method using PEG 8000 as a precipitant. The crystals belong to space group P21 (pVIPR peptide) or P212121 (pLMP2 peptide). Data sets were collected to 1.55 Å (B*2703–pVIPR) or 2.0 Å (B*2703–pLMP2) resolution using synchrotron radiation. With B*2705–pVIPR as a search model, a clear molecular‐replacement solution was found for both B*2703 complexes.

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