spacer CRYSTAL STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN H IN COMPLEX WITH HUMAN MHC CLASS II
Primary citation
Title Crystal Structure of a Superantigen Bound to MHC Class II Displays Zinc and Peptide Dependence
Authors Petersson, K.search; Hakansson, M.search; Nilsson, H.search; Forsberg, G.search; Svensson, L.A.search; Liljas, A.search; Walse, B.search
Journal EMBO J.search vol:20, pag:3306-3312 (2001), Identifiers: PubMed ID (11432818)search DOI (10.1093/emboj/20.13.3306)
Abstract The three-dimensional structure of a bacterial superantigen, Staphylococcus aureus enterotoxin H (SEH), bound to human major histocompatibility complex (MHC) class II (HLA-DR1) has been determined by X-ray crystallography to 2.6 A resolution (1HXY). The superantigen binds on top of HLA-DR1 in a completely different way from earlier co-crystallized superantigens from S.aureus. SEH interacts with high affinity through a zinc ion with the beta1 chain of HLA-DR1 and also with the peptide presented by HLA-DR1. The structure suggests that all superantigens interacting with MHC class II in a zinc-dependent manner present the superantigen in a common way. This suggests a new model for ternary complex formation with the T-cell receptor (TCR), in which a contact between the TCR and the MHC class II is unlikely.
MeSH terms Amino Acid Sequencesearch, Binding Sitessearch, Cloningsearch, Molecularsearch, Crystallographysearch, X-Raysearch, Enterotoxinssearch, HLA-DR1 Antigensearch, Humanssearch, Modelssearch, Molecularsearch, Molecular Sequence Datasearch, Protein Conformationsearch, Protein Structuresearch, Secondarysearch, Protein Structuresearch, Tertiarysearch, Recombinant Proteinssearch, Sequence Alignmentsearch, Sequence Homologysearch, Amino Acidsearch, Staphylococcus aureussearch, Superantigenssearch, Zincsearch, Zinc Fingerssearch
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