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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.","bibjson":{"author":[{"initials":"NG","lastname":"Walpole","name":"Walpole NG"},{"initials":"L","lastname":"Kjer-Nielsen","name":"Kjer-Nielsen L"},{"initials":"L","lastname":"Kostenko","name":"Kostenko L"},{"initials":"J","lastname":"McCluskey","name":"McCluskey J"},{"initials":"AG","lastname":"Brooks","name":"Brooks AG"},{"initials":"J","lastname":"Rossjohn","name":"Rossjohn J"},{"initials":"CS","lastname":"Clements","name":"Clements CS"}],"identifier":[{"id":"10.1016/j.jmb.2010.01.052","type":"doi"},{"id":"20122941","type":"pubmed"}],"issue":["2"],"journal":{"iso_abbreviation":"J. Mol. 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