Crystal Structure of a Tyrosine Phosphorylated STAT-1 Dimer Bound to DNA
Copyright policy )Crystal Structure of a Tyrosine Phosphorylated STAT-1 Dimer Bound to DNA
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.
- The Rockefeller University
- Rockefeller University United States
- Rockefeller University United States
- Howard Hughes Medical Institute United States
Models, Molecular, Crystallography, Sequence Homology, Amino Acid, Biochemistry, Genetics and Molecular Biology(all), Molecular Sequence Data, Molecular Conformation, NF-kappa B, DNA, Peptide Fragments, Recombinant Proteins, Protein Structure, Tertiary, DNA-Binding Proteins, STAT1 Transcription Factor, Oligodeoxyribonucleotides, Humans, Amino Acid Sequence, Phosphorylation, Phosphotyrosine, Dimerization, Synchrotrons, Protein Binding
Models, Molecular, Crystallography, Sequence Homology, Amino Acid, Biochemistry, Genetics and Molecular Biology(all), Molecular Sequence Data, Molecular Conformation, NF-kappa B, DNA, Peptide Fragments, Recombinant Proteins, Protein Structure, Tertiary, DNA-Binding Proteins, STAT1 Transcription Factor, Oligodeoxyribonucleotides, Humans, Amino Acid Sequence, Phosphorylation, Phosphotyrosine, Dimerization, Synchrotrons, Protein Binding
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