z-logo
open-access-imgOpen Access
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
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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom