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

doi:10.1038/nsmb1193

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 journal › Article › peer-review

38 Scopus citations

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 language	English (US)
Pages (from-to)	169-171
Number of pages	3
Journal	Nature Structural and Molecular Biology
Volume	14
Issue number	2
DOIs	https://doi.org/10.1038/nsmb1193
State	Published - Feb 2007
Externally published	Yes

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1038/nsmb1193

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@article{f88b0e544a024c5590109929f5f0f35d,

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

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-{\AA} 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.",

author = "Limin Wang and Yiwei Zhao and Zhong Li and Yi Guo and Jones, \{Lindsay L.\} and Kranz, \{David M.\} and Walid Mourad and Hongmin Li",

note = "Funding Information: 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.",

year = "2007",

month = feb,

doi = "10.1038/nsmb1193",

language = "English (US)",

volume = "14",

pages = "169--171",

journal = "Nature Structural and Molecular Biology",

issn = "1545-9993",

publisher = "Nature Research",

number = "2",

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TY - JOUR

T1 - Crystal structure of a complete ternary complex of TCR, superantigen and peptide-MHC

AU - Wang, Limin

AU - Zhao, Yiwei

AU - Li, Zhong

AU - Guo, Yi

AU - Jones, Lindsay L.

AU - Kranz, David M.

AU - Mourad, Walid

AU - Li, Hongmin

N1 - Funding Information: 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.

PY - 2007/2

Y1 - 2007/2

N2 - '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.

AB - '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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AN - SCOPUS:33846977011

SN - 1545-9993

VL - 14

SP - 169

EP - 171

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

IS - 2

ER -

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

Abstract

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