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  Preliminary X-ray diffraction analysis of crystals from the recombinantly expressed human major histocompatibility antigen HLA-B*2704 in complex with a viral peptide and with a self-peptide

Loll, B., Zawacka, A., Biesiadka, J., Petter, C., Rueckert, C., Saenger, W., et al. (2005). Preliminary X-ray diffraction analysis of crystals from the recombinantly expressed human major histocompatibility antigen HLA-B*2704 in complex with a viral peptide and with a self-peptide. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 61(10), 939-941. doi:10.1107/S1744309105029234.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0002-50F1-3 Version Permalink: http://hdl.handle.net/21.11116/0000-0002-50F2-2
Genre: Journal Article

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ActaCrysF_61_2005_939.pdf (Any fulltext), 145KB
 
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 Creators:
Loll, Bernhard1, Author              
Zawacka, Anna, Author
Biesiadka, Jacek, Author
Petter, Cordula, Author
Rueckert, Christine, Author
Saenger, Wolfram, Author
Uchanska−Ziegler, Barbara, Author
Ziegler, Andreas, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: HLA-B27 subtypes; HLA-B*2704; subtype-dependent peptide-binding modes; ankylosing spondylitis; polymorphism
 Abstract: The product of the human leukocyte antigen (HLA) gene HLA-B*2704 differs from that of the prototypical subtype HLA-B*2705 by three amino acids at heavy-chain residues 77 (Ser instead of Asp), 152 (Glu instead of Val) and 211 (Gly instead of Ala). In contrast to the ubiquitous HLA-B*2705 subtype, HLA-B*2704 occurs only in orientals. Both subtypes are strongly associated with spondyloarthropathies and the peptides presented by these subtypes are suspected to play a role in disease pathogenesis. HLA-B*2704 was crystallized in complex with a viral peptide and with a self-peptide using the hanging-drop vapour-diffusion method with PEG as a precipitant. Both crystals belong to space group P2(1)2(1)2(1). Data sets were collected to 1.60 A (complex with the self-peptide pVIPR) or to 1.90 A (complex with the viral peptide pLMP2) resolution using synchrotron radiation. With HLA-B*2705 complexed with pVIPR as a search model, unambiguous molecular-replacement solutions were found for the complexes of HLA-B*2704 with both peptides.

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Language(s): eng - English
 Dates: 2005-07-202005-09-142005-09-302005-10-01
 Publication Status: Published in print
 Pages: 3
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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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 (10) Sequence Number: - Start / End Page: 939 - 941 Identifier: ISSN: 1744-3091
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000017210_1