| pubmed-article:20122941 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20122941 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:20122941 | lifeskim:mentions | umls-concept:C1415587 | lld:lifeskim |
| pubmed-article:20122941 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:20122941 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:20122941 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:20122941 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:20122941 | lifeskim:mentions | umls-concept:C2825311 | lld:lifeskim |
| pubmed-article:20122941 | lifeskim:mentions | umls-concept:C0349590 | lld:lifeskim |
| pubmed-article:20122941 | lifeskim:mentions | umls-concept:C2349209 | lld:lifeskim |
| pubmed-article:20122941 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:20122941 | pubmed:dateCreated | 2010-3-8 | lld:pubmed |
| pubmed-article:20122941 | pubmed:abstractText | The highly polymorphic major histocompatibility complex class Ia (MHC-Ia) molecules present a broad array of peptides to the clonotypically diverse alphabeta T-cell receptors. In contrast, MHC-Ib molecules exhibit limited polymorphism and bind a more restricted peptide repertoire, in keeping with their major role in innate immunity. Nevertheless, some MHC-Ib molecules do play a role in adaptive immunity. While human leukocyte antigen E (HLA-E), the MHC-Ib molecule, binds a very restricted repertoire of peptides, the peptide binding preferences of HLA-G, the class Ib molecule, are less stringent, although the basis by which HLA-G can bind various peptides is unclear. To investigate how HLA-G can accommodate different peptides, we compared the structure of HLA-G bound to three naturally abundant self-peptides (RIIPRHLQL, KGPPAALTL and KLPQAFYIL) and their thermal stabilities. The conformation of HLA-G(KGPPAALTL) was very similar to that of the HLA-G(RIIPRHLQL) structure. However, the structure of HLA-G(KLPQAFYIL) not only differed in the conformation of the bound peptide but also caused a small shift in the alpha2 helix of HLA-G. Furthermore, the relative stability of HLA-G was observed to be dependent on the nature of the bound peptide. These peptide-dependent effects on the substructure of the monomorphic HLA-G are likely to impact on its recognition by receptors of both innate and adaptive immune systems. | lld:pubmed |
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| pubmed-article:20122941 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20122941 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20122941 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20122941 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20122941 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20122941 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:20122941 | pubmed:issn | 1089-8638 | lld:pubmed |
| pubmed-article:20122941 | pubmed:author | pubmed-author:BrooksAndrew... | lld:pubmed |
| pubmed-article:20122941 | pubmed:author | pubmed-author:McCluskeyJame... | lld:pubmed |
| pubmed-article:20122941 | pubmed:author | pubmed-author:ClementsCraig... | lld:pubmed |
| pubmed-article:20122941 | pubmed:author | pubmed-author:Kjer-NielsenL... | lld:pubmed |
| pubmed-article:20122941 | pubmed:author | pubmed-author:RossjohnJamie... | lld:pubmed |
| pubmed-article:20122941 | pubmed:author | pubmed-author:KostenkoLyudm... | lld:pubmed |
| pubmed-article:20122941 | pubmed:author | pubmed-author:WalpoleNichol... | lld:pubmed |
| pubmed-article:20122941 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20122941 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:20122941 | pubmed:volume | 397 | lld:pubmed |
| pubmed-article:20122941 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20122941 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20122941 | pubmed:pagination | 467-80 | lld:pubmed |
| pubmed-article:20122941 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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