Crystal structure of a complete ternary complex of TCR, superantigen and peptide-MHC

Limin Wang, Yiwei Zhao, Zhong Li, Yi Guo, Lindsay L. Jones, David M Kranz, Walid Mourad, Hongmin Li

Research output: Contribution to journalArticle

Abstract

'Superantigens' (SAgs) trigger the massive activation of T cells by simultaneous interactions with MHC and TCR receptors, leading to human diseases. Here we present the first crystal structure, at 2.5-Å resolution, of a complete ternary complex between a SAg and its two receptors, HLA-DR1/HA and TCR. The most striking finding is that the SAg Mycoplasma arthritidis mitogen, unlike others, has direct contacts not only with TCR Vβ but with TCR Vα.

Original languageEnglish (US)
Pages (from-to)169-171
Number of pages3
JournalNature Structural and Molecular Biology
Volume14
Issue number2
DOIs
StatePublished - Feb 2007

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HLA-DR1 Antigen
Superantigens
Cell Communication
T-Lymphocytes
Peptides
Mycoplasma arthritidis mitogen

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

Crystal structure of a complete ternary complex of TCR, superantigen and peptide-MHC. / Wang, Limin; Zhao, Yiwei; Li, Zhong; Guo, Yi; Jones, Lindsay L.; Kranz, David M; Mourad, Walid; Li, Hongmin.

In: Nature Structural and Molecular Biology, Vol. 14, No. 2, 02.2007, p. 169-171.

Research output: Contribution to journalArticle

Wang, Limin ; Zhao, Yiwei ; Li, Zhong ; Guo, Yi ; Jones, Lindsay L. ; Kranz, David M ; Mourad, Walid ; Li, Hongmin. / Crystal structure of a complete ternary complex of TCR, superantigen and peptide-MHC. In: Nature Structural and Molecular Biology. 2007 ; Vol. 14, No. 2. pp. 169-171.
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