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.

The product of the human leukocyte antigen (HLA) gene HLA-B2703 differs from that of the prototypical subtype HLA-B2705 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 B2703-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 (B2703-pVIPR) or 2.0 A (B2703-pLMP2) resolution using synchrotron radiation. With B2705-pVIPR as a search model, a clear molecular-replacement solution was found for both B*2703 complexes.