1SBB
T-CELL RECEPTOR BETA CHAIN COMPLEXED WITH SUPERANTIGEN SEB
Summary for 1SBB
Entry DOI | 10.2210/pdb1sbb/pdb |
Descriptor | PROTEIN (14.3.D T CELL ANTIGEN RECEPTOR), PROTEIN (STAPHYLOCOCCAL ENTEROTOXIN B) (3 entities in total) |
Functional Keywords | t cell receptor, superantigen, complex, immune system |
Biological source | Mus musculus (house mouse) More |
Cellular location | Secreted: P01552 |
Total number of polymer chains | 4 |
Total formula weight | 109959.11 |
Authors | Li, H.,Mariuzza, R.A. (deposition date: 1999-02-22, release date: 1999-03-01, Last modification date: 2024-11-20) |
Primary citation | Li, H.,Llera, A.,Tsuchiya, D.,Leder, L.,Ysern, X.,Schlievert, P.M.,Karjalainen, K.,Mariuzza, R.A. Three-dimensional structure of the complex between a T cell receptor beta chain and the superantigen staphylococcal enterotoxin B. Immunity, 9:807-816, 1998 Cited by PubMed 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. PubMed: 9881971DOI: 10.1016/S1074-7613(00)80646-9 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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