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Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA.

The Fos and Jun families of eukaryotic transcription factors heterodimerize to form complexes capable of binding 5'-TGAGTCA-3' DNA elements. We have determined the X-ray crystal structure of a heterodimer of the bZIP regions of c-Fos and c-Jun bound to DNA. Both subunits form continuous alpha-helices. The carboxy-terminal regions form an asymmetric coiled-coil, and the amino-terminal regions make base-specific contacts with DNA in the major groove. Comparison of the two crystallographically distinct protein-DNA complexes show that the coiled-coil is flexibly joined to the basic regions and that the Fos-Jun heterodimer does not recognize the asymmetric 5'-TGAGTCA-3' recognition element in a unique orientation. There is an extensive network of electrostatic interactions between subunits within the coiled-coil, consistent with proposals that these interactions determine preferential formation of the heterodimer over either of the homodimers.

Pubmed ID: 7816143


  • Glover JN
  • Harrison SC



Publication Data

January 19, 1995

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Base Sequence
  • Crystallography, X-Ray
  • DNA
  • Humans
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Protein Binding
  • Protein Conformation
  • Proto-Oncogene Proteins c-fos
  • Proto-Oncogene Proteins c-jun
  • Transcription Factor AP-1