Open AccessPurification, 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
Author(s) -
Loll Bernhard,
Zawacka Anna,
Biesiadka Jacek,
Rückert Christine,
Volz Armin,
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/s1744309105007438
Subject(s) - peptide , human leukocyte antigen , crystallization , major histocompatibility complex , hla a , antigen , histocompatibility , hla b , x ray crystallography , biology , microbiology and biotechnology , chemistry , diffraction , biochemistry , immunology , physics , optics , organic chemistry
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 P 2 1 (pVIPR peptide) or P 2 1 2 1 2 1 (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.