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 publicationJournal articleAcademic researchpeer-review

536 Citations (Scopus)


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 languageEnglish
Pages (from-to)827-839
Number of pages13
Issue number5
Publication statusPublished - 29 May 1998
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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