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.
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
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
Cell
Date: May. 29, 1998
PubMed ID: 9630226
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