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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Apr 1;61(Pt 4):372-4. doi: 10.1107/S1744309105007438. Epub 2005 Mar 12.

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 P2(1) (pVIPR peptide) or P2(1)2(1)2(1) (pLMP2 peptide). Data sets were collected to 1.55 A (B*2703-pVIPR) or 2.0 A (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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigen-Antibody Complex / chemistry*
  • Antigens, Viral / chemistry
  • Autoantigens / chemistry
  • Crystallization / methods
  • HLA-B Antigens / chemistry*
  • HLA-B Antigens / immunology
  • HLA-B27 Antigen
  • Humans
  • Peptide Fragments / chemistry
  • Peptide Fragments / immunology
  • Viral Proteins / chemistry
  • Volatilization
  • X-Ray Diffraction

Substances

  • Antigen-Antibody Complex
  • Antigens, Viral
  • Autoantigens
  • HLA-B Antigens
  • HLA-B*27:03 antigen
  • HLA-B27 Antigen
  • Peptide Fragments
  • Viral Proteins