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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Oct 1;61(Pt 10):939-41. doi: 10.1107/S1744309105029234. Epub 2005 Sep 30.

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 P2(1)2(1)2(1). Data sets were collected to 1.60 A (complex with the self-peptide pVIPR) or to 1.90 A (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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / metabolism
  • Glutathione / chemistry
  • HLA Antigens / chemistry*
  • HLA-B Antigens / chemistry*
  • HLA-B27 Antigen
  • Humans
  • Major Histocompatibility Complex
  • Mutagenesis
  • Peptides / chemistry
  • Protein Conformation
  • Recombinant Proteins / chemistry*
  • X-Ray Diffraction

Substances

  • HLA Antigens
  • HLA-B Antigens
  • HLA-B*27:04 antigen
  • HLA-B27 Antigen
  • Peptides
  • Recombinant Proteins
  • Glutathione