spacer Crystal structure of the D227A variant of Staphylococcal enterotoxin A in complex with human MHC class II
Primary citation
Title Crystal Structure of a SEA Variant in Complex with MHC Class II Reveals the Ability of SEA to Crosslink MHC Molecules
Authors Petersson, K.search; Thunnissen, M.search; Forsberg, G.search; Walse, B.search
Journal STRUCTUREsearch vol:10, pag:1619-1626 (2002), Identifiers: PubMed ID (12467569)search DOI (10.1016/S0969-2126(02)00895-X)
Abstract Although the biological properties of staphylococcal enterotoxin A (SEA) have been well characterized, structural insights into the interaction between SEA and major histocompatibilty complex (MHC) class II have only been obtained by modeling. Here, the crystal structure of the D227A variant of SEA in complex with human MHC class II has been determined by X-ray crystallography. SEA(D227A) exclusively binds with its N-terminal domain to the alpha chain of HLA-DR1. The ability of one SEA molecule to crosslink two MHC molecules was modeled. It shows that this SEA molecule cannot interact with the T cell receptor (TCR) while a second SEA molecule interacts with MHC. Because of its relatively low toxicity, the D227A variant of SEA is used in tumor therapy.
MeSH terms Amino Acid Sequencesearch, Crystallographysearch, X-Raysearch, Enterotoxinssearch, Histocompatibility Antigens Class IIsearch, Lymphocyte Activationsearch, Modelssearch, Molecularsearch, Molecular Sequence Datasearch, Protein Conformationsearch, Receptorssearch, Antigensearch, T-Cellsearch, Recombinant Proteinssearch
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