TI  - Crystal structure of the heterodimeric bZIP transcription factor
       <prot>c-Fos</prot> - <prot>c-Jun</prot>  bound to DNA.
PG  - 257-61
AB  - The  <prot>Fos</prot>  and  <prot>Jun</prot>  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  <prot>c-Fos</prot>  and  <prot>c-Jun</prot>  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  <prot>Fos</prot> - <prot>Jun</prot>  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.
AD  - Howard Hughes Medical Institute, Harvard University, Cambridge,
