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 |
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Pages (from-to) | 827-839 |
Number of pages | 13 |
Journal | Cell |
Volume | 93 |
Issue number | 5 |
DOIs | |
Publication status | Published - 29 May 1998 |
Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)