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.
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
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
Nature
Date: Jan. 19, 1995
PubMed ID: 7816143
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