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http://purl.uniprot.org/citations/20122941http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20122941http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20122941http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/20122941http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2010.01.052"xsd:string
http://purl.uniprot.org/citations/20122941http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2010.01.052"xsd:string
http://purl.uniprot.org/citations/20122941http://purl.uniprot.org/core/author"Rossjohn J."xsd:string
http://purl.uniprot.org/citations/20122941http://purl.uniprot.org/core/author"Rossjohn J."xsd:string
http://purl.uniprot.org/citations/20122941http://purl.uniprot.org/core/author"Brooks A.G."xsd:string
http://purl.uniprot.org/citations/20122941http://purl.uniprot.org/core/author"Brooks A.G."xsd:string
http://purl.uniprot.org/citations/20122941http://purl.uniprot.org/core/author"Clements C.S."xsd:string
http://purl.uniprot.org/citations/20122941http://purl.uniprot.org/core/author"Clements C.S."xsd:string
http://purl.uniprot.org/citations/20122941http://purl.uniprot.org/core/author"Kjer-Nielsen L."xsd:string
http://purl.uniprot.org/citations/20122941http://purl.uniprot.org/core/author"Kjer-Nielsen L."xsd:string
http://purl.uniprot.org/citations/20122941http://purl.uniprot.org/core/author"McCluskey J."xsd:string
http://purl.uniprot.org/citations/20122941http://purl.uniprot.org/core/author"McCluskey J."xsd:string
http://purl.uniprot.org/citations/20122941http://purl.uniprot.org/core/author"Kostenko L."xsd:string
http://purl.uniprot.org/citations/20122941http://purl.uniprot.org/core/author"Kostenko L."xsd:string
http://purl.uniprot.org/citations/20122941http://purl.uniprot.org/core/author"Walpole N.G."xsd:string
http://purl.uniprot.org/citations/20122941http://purl.uniprot.org/core/author"Walpole N.G."xsd:string
http://purl.uniprot.org/citations/20122941http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20122941http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20122941http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/20122941http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/20122941http://purl.uniprot.org/core/pages"467-480"xsd:string
http://purl.uniprot.org/citations/20122941http://purl.uniprot.org/core/pages"467-480"xsd:string