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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

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.

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ActaCrysF_61_2005_372.pdf (Any fulltext), 205KB
 
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 Creators:
Loll, Bernhard1, Author           
Zawacka, Anna, Author
Biesiadka, Jacek, Author
Rueckert, Christine, Author
Volz, Armin, Author
Saenger, Wolfram, Author
Uchanska-Ziegler, Barbara, Author
Ziegler, Andreas, Author
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: HLA-B*2703; HLA-B27 subtypes; subtype-dependent peptide-binding modes; ankylosing spondylitis; residue 59 polymorphism
 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.

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Language(s): eng - English
 Dates: 2005-01-232005-03-082005-03-122005-04-01
 Publication Status: Issued
 Pages: 3
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Source Genre: Journal
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Publ. Info: Blackwell Publishing Limited
Pages: - Volume / Issue: 61 (4) Sequence Number: - Start / End Page: 372 - 374 Identifier: ISSN: 1744-3091
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000017210_1