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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

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons94115

Loll,  Bernhard
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Loll, B., Zawacka, A., Biesiadka, J., Rueckert, C., Volz, A., Saenger, W., et al. (2005). 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, 61(4), 372-374. doi:10.1107/S1744309105007438.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-9BF1-6
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 P21 (pVIPR peptide) or P212121 (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