Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA

Xiaomin Chen; Uwe Vinkemeier; Yanxiang Zhao; David Jeruzalmi; James E. Darnell; John Kuriyan

doi:10.1016/S0092-8674(00)81443-9

Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA

Xiaomin Chen, Uwe Vinkemeier, Yanxiang Zhao, David Jeruzalmi, James E. Darnell, John Kuriyan

Research output: Journal article publication › Journal article › Academic research › peer-review

508 Citations (Scopus)

Abstract

The crystal structure of the DNA complex of a STAT-1 homodimer has been determined at 2.9 Å resolution. STAT-1 utilizes a DNA-binding domain with an immunoglobulin fold, similar to that of NFκB and the p53 tumor suppressor protein. The STAT-1 dimer forms a contiguous C-shaped clamp around DNA that is stabilized by reciprocal and highly specific interactions between the SH2 domain of one monomer and the C-terminal segment, phosphorylated on tyrosine, of the other. The phosphotyrosine-binding site of the SH2 domain in each monomer is coupled structurally to the DNA-binding domain, suggesting a potential role for the SH2-phosphotyrosine interaction in the stabilization of DNA interacting elements.

Original language	English
Pages (from-to)	827-839
Number of pages	13
Journal	Cell
Volume	93
Issue number	5
DOIs	https://doi.org/10.1016/S0092-8674(00)81443-9
Publication status	Published - 29 May 1998
Externally published	Yes

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

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10.1016/S0092-8674(00)81443-9

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title = "Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA",

abstract = "The crystal structure of the DNA complex of a STAT-1 homodimer has been determined at 2.9 {\AA} resolution. STAT-1 utilizes a DNA-binding domain with an immunoglobulin fold, similar to that of NFκB and the p53 tumor suppressor protein. The STAT-1 dimer forms a contiguous C-shaped clamp around DNA that is stabilized by reciprocal and highly specific interactions between the SH2 domain of one monomer and the C-terminal segment, phosphorylated on tyrosine, of the other. The phosphotyrosine-binding site of the SH2 domain in each monomer is coupled structurally to the DNA-binding domain, suggesting a potential role for the SH2-phosphotyrosine interaction in the stabilization of DNA interacting elements.",

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AU - Chen, Xiaomin

AU - Vinkemeier, Uwe

AU - Zhao, Yanxiang

AU - Jeruzalmi, David

AU - Darnell, James E.

AU - Kuriyan, John

PY - 1998/5/29

Y1 - 1998/5/29

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AB - The crystal structure of the DNA complex of a STAT-1 homodimer has been determined at 2.9 Å resolution. STAT-1 utilizes a DNA-binding domain with an immunoglobulin fold, similar to that of NFκB and the p53 tumor suppressor protein. The STAT-1 dimer forms a contiguous C-shaped clamp around DNA that is stabilized by reciprocal and highly specific interactions between the SH2 domain of one monomer and the C-terminal segment, phosphorylated on tyrosine, of the other. The phosphotyrosine-binding site of the SH2 domain in each monomer is coupled structurally to the DNA-binding domain, suggesting a potential role for the SH2-phosphotyrosine interaction in the stabilization of DNA interacting elements.

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DO - 10.1016/S0092-8674(00)81443-9

M3 - Journal article

C2 - 9630226

VL - 93

SP - 827

EP - 839

JO - Cell

JF - Cell

SN - 0092-8674

IS - 5

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Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA

Abstract

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