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5def

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== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
[[http://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
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== Publication Abstract from PubMed ==
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OBJECTIVE: Dissimilarities in antigen processing and presentation are known to contribute to the differential association of HLA-B*27 subtypes with the inflammatory rheumatic disease ankylosing spondylitis (AS). In support of this contention, previous X-ray crystallographic data showed that peptides can be displayed by almost identical HLA-B*27 molecules in a subtype-dependent manner, allowing cytotoxic T lymphocytes to distinguish between these subtypes. For example, the human self-peptide pVIPR (RRKWRRWHL) is displayed in a single conformation by B*27:09 (not AS-associated), while B*27:05 (AS-associated) presents the peptide in a dual binding mode. In addition, differences in conformational flexibility between these subtypes might affect their stability or antigen presentation capability. We investigated B*27:04 and B*27:06, another pair of minimally distinct HLA-B*27 subtypes, to assess whether dual peptide conformations or structural dynamics could play a role in the initiation of AS. METHODS: Using X-ray crystallography, we solved the structures of pVIPR-B*27:04 and pVIPR-B*27:06 and employed isotope-edited infrared (IR) spectroscopy to probe the dynamics of these HLA-B*27 subtypes. RESULTS: As opposed to B*27:05 and B*27:09, B*27:04 (AS-associated) displays pVIPR conventionally and B*27:06 (not AS-associated) presents the peptide in a dual conformation. On the other hand, the comparison of the four HLA-B*27 subtypes using IR spectroscopy revealed that B*27:04 and B*27:05 exhibit elevated molecular dynamics when compared to the non-associated subtypes B*27:06 and B*27:09. CONCLUSION: Our results demonstrate that an increase in conformational flexibility characterizes the disease-associated subtypes B*27:04 and B*27:05. This article is protected by copyright. All rights reserved.
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Increased conformational flexibility characterizes HLA-B*27 subtypes associated with ankylosing spondylitis.,Loll B, Fabian H, Huser H, Hee CS, Ziegler A, Uchanska-Ziegler B, Ziegler A Arthritis Rheumatol. 2016 Jan 8. doi: 10.1002/art.39567. PMID:26748477<ref>PMID:26748477</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
== References ==
<references/>
<references/>

Revision as of 08:59, 20 January 2016

Crystal structure of B*27:04 complex bound to the pVIPR peptide

5def, resolution 1.60Å

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