{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,26]],"date-time":"2026-03-26T02:34:41Z","timestamp":1774492481009,"version":"3.50.1"},"reference-count":52,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2016,4,27]],"date-time":"2016-04-27T00:00:00Z","timestamp":1461715200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Arthritis &amp; Rheumatology"],"published-print":{"date-parts":[[2016,5]]},"abstract":"<jats:sec><jats:title>Objective<\/jats:title><jats:p>Dissimilarities in antigen processing and presentation are known to contribute to the differential association of HLA\u2013B*27 subtypes with the inflammatory rheumatic disease ankylosing spondylitis (AS). In support of this notion, previous x\u2010ray crystallographic data showed that peptides can be displayed by almost identical HLA\u2013B*27 molecules in a subtype\u2010dependent manner, allowing cytotoxic T lymphocytes to distinguish between these subtypes. For example, a human self\u2010peptide derived from vasoactive intestinal peptide receptor type 1 (pVIPR; sequence RRKWRRWHL) is displayed in a single conformation by B*27:09 (which is not associated with AS), while B*27:05 (which is associated with AS) 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. This study was undertaken to investigate B*27:04 and B*27:06, another pair of minimally distinct HLA\u2013B*27 subtypes, to assess whether dual peptide conformations or structural dynamics play a role in the initiation of AS.<\/jats:p><\/jats:sec><jats:sec><jats:title>Methods<\/jats:title><jats:p>Using x\u2010ray crystallography, we determined the structures of the pVIPR\u2013B*27:04 and pVIPR\u2013B*27:06 complexes and used isotope\u2010edited infrared (IR) spectroscopy to probe the dynamics of these HLA\u2013B*27 subtypes.<\/jats:p><\/jats:sec><jats:sec><jats:title>Results<\/jats:title><jats:p>As opposed to B*27:05 and B*27:09, B*27:04 (which is associated with AS) displays pVIPR conventionally and B*27:06 (which is not associated with AS) presents the peptide in a dual conformation. Comparison of the 4 HLA\u2013B*27 subtypes using IR spectroscopy revealed that B*27:04 and B*27:05 possess elevated molecular dynamics compared to the nonassociated subtypes B*27:06 and B*27:09.<\/jats:p><\/jats:sec><jats:sec><jats:title>Conclusion<\/jats:title><jats:p>Our results demonstrate that an increase in conformational flexibility characterizes the disease\u2010associated subtypes B*27:04 and B*27:05.<\/jats:p><\/jats:sec>","DOI":"10.1002\/art.39567","type":"journal-article","created":{"date-parts":[[2016,1,10]],"date-time":"2016-01-10T12:33:46Z","timestamp":1452429226000},"page":"1172-1182","source":"Crossref","is-referenced-by-count":35,"title":["Increased Conformational Flexibility of HLA\u2013B*27 Subtypes Associated With Ankylosing Spondylitis"],"prefix":"10.1002","volume":"68","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7928-4488","authenticated-orcid":false,"given":"Bernhard","family":"Loll","sequence":"first","affiliation":[{"name":"Freie Universit\u00e4t Berlin 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