1FOS

TWO HUMAN C-FOS:C-JUN:DNA COMPLEXES

Summary for 1FOS

• Entry DOI: 10.2210/pdb1fos/pdb
• Descriptor: DNA (5'-D(*AP*AP*TP*GP*GP*AP*TP*GP*AP*GP*TP*CP*AP*TP*AP*GP*GP*AP*GP*A)-3'), DNA (5'-D(*TP*TP*CP*TP*CP*CP*TP*AP*TP*GP*AP*CP*TP*CP*AP*TP*CP*CP*AP*T)-3'), P55-C-FOS PROTO-ONCOGENE PROTEIN, ... (4 entities in total)
• Functional Keywords: coiled-coil, dna-binding protein, heterodimer, transcription-dna complex, transcription/dna
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P01100
• Total number of polymer chains: 8
• Total formula weight: 53934.24

Authors

Glover, J.N.M.,Harrison, S.C. (deposition date: 1995-03-07, release date: 1995-07-10, Last modification date: 2024-02-07)

Primary citation

Glover, J.N.,Harrison, S.C.
Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA.
Nature, 373:257-261, 1995

PubMed Abstract: 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: 7816143
DOI: 10.1038/373257a0

Experimental method

X-RAY DIFFRACTION (3.05 Å)