| pubmed-article:14734527 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14734527 | lifeskim:mentions | umls-concept:C0019740 | lld:lifeskim |
| pubmed-article:14734527 | lifeskim:mentions | umls-concept:C0026377 | lld:lifeskim |
| pubmed-article:14734527 | lifeskim:mentions | umls-concept:C1554184 | lld:lifeskim |
| pubmed-article:14734527 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:14734527 | pubmed:dateCreated | 2004-1-21 | lld:pubmed |
| pubmed-article:14734527 | pubmed:abstractText | The products of the human leukocyte antigen subtypes HLA-B*2705 and HLA-B*2709 differ only in residue 116 (Asp vs. His) within the peptide binding groove but are differentially associated with the autoimmune disease ankylosing spondylitis (AS); HLA-B*2705 occurs in AS-patients, whereas HLA-B*2709 does not. The subtypes also generate differential T cell repertoires as exemplified by distinct T cell responses against the self-peptide pVIPR (RRKWRRWHL). The crystal structures described here show that pVIPR binds in an unprecedented dual conformation only to HLA-B*2705 molecules. In one binding mode, peptide pArg5 forms a salt bridge to Asp116, connected with drastically different interactions between peptide and heavy chain, contrasting with the second, conventional conformation, which is exclusively found in the case of B*2709. These subtype-dependent differences in pVIPR binding link the emergence of dissimilar T cell repertoires in individuals with HLA-B*2705 or HLA-B*2709 to the buried Asp116/His116 polymorphism and provide novel insights into peptide presentation by major histocompatibility antigens. | lld:pubmed |
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| pubmed-article:14734527 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14734527 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14734527 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:14734527 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14734527 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:14734527 | pubmed:issn | 0022-1007 | lld:pubmed |
| pubmed-article:14734527 | pubmed:author | pubmed-author:ZieglerAndrea... | lld:pubmed |
| pubmed-article:14734527 | pubmed:author | pubmed-author:SaengerWolfra... | lld:pubmed |
| pubmed-article:14734527 | pubmed:author | pubmed-author:Uchanska-Zieg... | lld:pubmed |
| pubmed-article:14734527 | pubmed:author | pubmed-author:HülsmeyerMart... | lld:pubmed |
| pubmed-article:14734527 | pubmed:author | pubmed-author:SorrentinoRos... | lld:pubmed |
| pubmed-article:14734527 | pubmed:author | pubmed-author:FiorilloMaria... | lld:pubmed |
| pubmed-article:14734527 | pubmed:author | pubmed-author:BettosiniFran... | lld:pubmed |
| pubmed-article:14734527 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14734527 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:14734527 | pubmed:volume | 199 | lld:pubmed |
| pubmed-article:14734527 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14734527 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14734527 | pubmed:pagination | 271-81 | lld:pubmed |
| pubmed-article:14734527 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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