• Register
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.


Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.


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