5deg: Difference between revisions
No edit summary |
No edit summary |
||
| Line 11: | Line 11: | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/Q7YQB0_HUMAN Q7YQB0_HUMAN]] Involved in the presentation of foreign antigens to the immune system.[SAAS:SAAS00281819] [[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/Q7YQB0_HUMAN Q7YQB0_HUMAN]] Involved in the presentation of foreign antigens to the immune system.[SAAS:SAAS00281819] [[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. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5deg" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||