Three-dimensional structure of the complex between a T cell receptor beta chain and the superantigen staphylococcal enterotoxin B.

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TitleThree-dimensional structure of the complex between a T cell receptor beta chain and the superantigen staphylococcal enterotoxin B.
Publication TypeJournal Article
Year of Publication1998
AuthorsLi, H, Llera, A, Tsuchiya, D, Leder, L, Ysern, X, Schlievert, PM, Karjalainen, K, Mariuzza, RA
JournalImmunity
Volume9
Issue6
Pagination807-16
Date Published1998 Dec
ISSN1074-7613
KeywordsAnimals, Crystallography, X-Ray, Enterotoxins, Histocompatibility Antigens Class II, Mice, Models, Molecular, Peptide Fragments, Peptides, Protein Conformation, Receptors, Antigen, T-Cell, alpha-beta, Staphylococcus aureus, Superantigens
Abstract

Superantigens (SAGs) are a class of immunostimulatory proteins of bacterial or viral origin that activate T cells by binding to the V beta domain of the T cell antigen receptor (TCR). The three-dimensional structure of the complex between a TCR beta chain (mouse V beta8.2) and the SAG staphylococcal enterotoxin B (SEB) at 2.4 A resolution reveals why SEB recognizes only certain V beta families, as well as why only certain SAGs bind mouse V beta8.2. Models of the TCR-SEB-peptide/MHC class II complex indicate that V alpha interacts with the MHC beta chain in the TCR-SAG-MHC complex. The extent of the interaction is variable and is largely determined by the geometry of V alpha/V beta domain association. This variability can account for the preferential expression of certain V alpha regions among T cells reactive with SEB.

Alternate JournalImmunity
PubMed ID9881971
Grant ListAI36900 / AI / NIAID NIH HHS / United States
AI42937 / AI / NIAID NIH HHS / United States
RG2747 / RG / CSR NIH HHS / United States