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 Crystallographica. Section F, Structural Biology and Crystallization Communications
Bernhard LollAndreas Ziegler

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.

References

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Citations

Mar 3, 2006·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Bernhard LollAndreas Ziegler
Mar 3, 2006·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Anna ZawackaAndreas Ziegler
Jul 11, 2007·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Pravin KumarBarbara Uchanska-Ziegler

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