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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.

Pubmed ID: 9630226


  • Chen X
  • Vinkemeier U
  • Zhao Y
  • Jeruzalmi D
  • Darnell JE
  • Kuriyan J



Publication Data

May 29, 1998

Associated Grants


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