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

Nature Structural & Molecular Biology volume 14, pages 169–171 (2007)Cite this article

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.

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Figure 1: Crystal structure of scTCR–MAM–HLA-DR1/HA ternary complex.
Figure 2: Conformational changes in MAM and TCR upon complex formation.

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Acknowledgements

This research was supported by grants AI50628 (to H.L.) and AI064611 (to D.M.K.) from the US National Institutes of Health. W.M. is supported by grants from the Arthritis Society of Canada, the Canadian Arthritis Network and the Canadian Institutes of Health Research. We thank A. Verschoor for critical reading of the manuscript, L.J. Stern (University of Massachusetts Medical School) for the gift of HLA-DR1 expression plasmids, and core facilities at the Wadsworth Center, including the Peptide Synthesis, Molecular Genetics and Macromolecular Crystallography cores, for synthesis of the HA peptide, DNA sequencing and crystal evaluation. Data for this study were collected at beamline X4A of the National Synchrotron Light Source, which is supported by the US Department of Energy, by grants from the US National Institutes of Health and by the New York Structural Biology Center.

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Author notes

  1. Limin Wang and Yiwei Zhao: These authors contributed equally to this work.

Authors and Affiliations

  1. New York State Department of Health, Wadsworth Center, Albany, 12201, New York, USA

    Limin Wang, Yiwei Zhao, Zhong Li, Yi Guo & Hongmin Li

  2. Department of Biochemistry, University of Illinois, Urbana, 61801, Illinois, USA

    Lindsay L Jones & David M Kranz

  3. Université de Montréal, CHUM, Campus St-Luc, Montréal, H2X 1P1, Québec, Canada

    Walid Mourad

  4. Department of Biomedical Sciences, State University of New York, Albany, 12201, New York, USA

    Hongmin Li

Authors
  1. Limin Wang
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  2. Yiwei Zhao
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  4. Yi Guo
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  5. Lindsay L Jones
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  6. David M Kranz
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  8. Hongmin Li
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Correspondence to Hongmin Li.

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Supplementary information

Supplementary Fig. 1

Details of the MAM-scTCR interface. (PDF 707 kb)

Supplementary Table 1

Data collection and refinement statistics. (PDF 18 kb)

Supplementary Table 2

Interactions between TCR and MAM. (PDF 17 kb)

Supplementary Methods (PDF 65 kb)

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Wang, L., Zhao, Y., Li, Z. et al. Crystal structure of a complete ternary complex of TCR, superantigen and peptide-MHC. Nat Struct Mol Biol 14, 169–171 (2007). https://doi.org/10.1038/nsmb1193

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