1FOS

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


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.05 Å
  • R-Value Free: 0.321 
  • R-Value Work: 0.230 
  • R-Value Observed: 0.230 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

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

Glover, J.N.Harrison, S.C.

(1995) Nature 373: 257-261

  • DOI: https://doi.org/10.1038/373257a0
  • Primary Citation of Related Structures:  
    1FOS

  • 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.


  • Organizational Affiliation

    Howard Hughes Medical Institute, Harvard University, Cambridge, Massachusetts 02138.


Macromolecules

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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
P55-C-FOS PROTO-ONCOGENE PROTEIN
E, G
62Homo sapiensMutation(s): 1 
UniProt & NIH Common Fund Data Resources
Find proteins for P01100 (Homo sapiens)
Explore P01100 
Go to UniProtKB:  P01100
PHAROS:  P01100
GTEx:  ENSG00000170345 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP01100
Sequence Annotations
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
C-JUN PROTO-ONCOGENE PROTEIN
F, H
62Homo sapiensMutation(s): 1 
UniProt & NIH Common Fund Data Resources
Find proteins for P05412 (Homo sapiens)
Explore P05412 
Go to UniProtKB:  P05412
PHAROS:  P05412
GTEx:  ENSG00000177606 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP05412
Sequence Annotations
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  • Reference Sequence

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Entity ID: 1
MoleculeChains LengthOrganismImage
DNA (5'-D(*AP*AP*TP*GP*GP*AP*TP*GP*AP*GP*TP*CP*AP*TP*AP*GP*GP*AP*GP*A)-3')
A, C
20N/A
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains LengthOrganismImage
DNA (5'-D(*TP*TP*CP*TP*CP*CP*TP*AP*TP*GP*AP*CP*TP*CP*AP*TP*CP*CP*AP*T)-3')
B, D
20N/A
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.05 Å
  • R-Value Free: 0.321 
  • R-Value Work: 0.230 
  • R-Value Observed: 0.230 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 241.1α = 90
b = 48.69β = 90
c = 66γ = 90
Software Package:
Software NamePurpose
X-PLORrefinement
XDSdata reduction

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1995-07-10
    Type: Initial release
  • Version 1.1: 2008-05-22
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2021-11-03
    Changes: Database references
  • Version 1.4: 2024-02-07
    Changes: Data collection