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1SBB

T-CELL RECEPTOR BETA CHAIN COMPLEXED WITH SUPERANTIGEN SEB

Summary for 1SBB
Entry DOI10.2210/pdb1sbb/pdb
DescriptorPROTEIN (14.3.D T CELL ANTIGEN RECEPTOR), PROTEIN (STAPHYLOCOCCAL ENTEROTOXIN B) (3 entities in total)
Functional Keywordst cell receptor, superantigen, complex, immune system
Biological sourceMus musculus (house mouse)
More
Cellular locationSecreted: P01552
Total number of polymer chains4
Total formula weight109959.11
Authors
Li, H.,Mariuzza, R.A. (deposition date: 1999-02-22, release date: 1999-03-01, Last modification date: 2024-11-20)
Primary citationLi, 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: 9881971
DOI: 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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