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

被引:156
作者
Li, HM
Llera, A
Tsuchiya, D
Leder, L
Ysern, X
Schlievert, PM
Karjalainen, K
Mariuzza, RA
机构
[1] Univ Maryland, Maryland Biotechnol Inst, Ctr Adv Res Biotechnol, Rockville, MD 20850 USA
[2] US FDA, Ctr Drug Evaluat & Res, Rockville, MD 20857 USA
[3] Univ Minnesota, Sch Med, Dept Microbiol, Minneapolis, MN 55455 USA
[4] Basel Inst Immunol, CH-4005 Basel, Switzerland
关键词
D O I
10.1016/S1074-7613(00)80646-9
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
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 beta 8.2) and the SAG staphylococcal enterotoxin B (SEB) at 2.4 Angstrom resolution reveals why SEE recognizes only certain V beta families, as well as why only certain SAGs bind mouse V beta 8.2. 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 SEE.
引用
收藏
页码:807 / 816
页数:10
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