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

Cell | May 29, 1998

The crystal structure of the DNA complex of a STAT-1 homodimer has been determined at 2.9 A resolution. STAT-1 utilizes a DNA-binding domain with an immunoglobulin fold, similar to that of NFkappaB 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.

Pubmed ID: 9630226 RIS Download

Mesh terms: Amino Acid Sequence | Crystallography | DNA | DNA-Binding Proteins | Dimerization | Humans | Models, Molecular | Molecular Conformation | Molecular Sequence Data | NF-kappa B | Oligodeoxyribonucleotides | Peptide Fragments | Phosphorylation | Phosphotyrosine | Protein Binding | Protein Structure, Tertiary | Recombinant Proteins | STAT1 Transcription Factor | Sequence Homology, Amino Acid | Synchrotrons | Trans-Activators | Tumor Suppressor Protein p53 | src Homology Domains

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