1A02

STRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN BOUND TO DNA


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.303 
  • R-Value Work: 0.246 
  • R-Value Observed: 0.246 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA.

Chen, L.Glover, J.N.Hogan, P.G.Rao, A.Harrison, S.C.

(1998) Nature 392: 42-48

  • DOI: https://doi.org/10.1038/32100
  • Primary Citation of Related Structures:  
    1A02

  • PubMed Abstract: 

    The nuclear factor of activated T cells (NFAT) and the AP-1 heterodimer, Fos-Jun, cooperatively bind a composite DNA site and synergistically activate the expression of many immune-response genes. A 2.7-A-resolution crystal structure of the DNA-binding domains of NFAT, Fos and Jun, in a quaternary complex with a DNA fragment containing the distal antigen-receptor response element from the interleukin-2 gene promoter, shows an extended interface between NFAT and AP-1, facilitated by the bending of Fos and DNA. The tight association of the three proteins on DNA creates a continuous groove for the recognition of 15 base pairs.


  • Organizational Affiliation

    Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, USA. lchen@xta1200.harvard.edu


Macromolecules

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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
NUCLEAR FACTOR OF ACTIVATED T CELLSC [auth N]301Homo sapiensMutation(s): 0 
Gene Names: NFAT1
UniProt & NIH Common Fund Data Resources
Find proteins for Q13469 (Homo sapiens)
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Go to UniProtKB:  Q13469
PHAROS:  Q13469
GTEx:  ENSG00000101096 
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UniProt GroupQ13469
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
AP-1 FRAGMENT FOSD [auth F]56Homo sapiensMutation(s): 2 
UniProt & NIH Common Fund Data Resources
Find proteins for P01100 (Homo sapiens)
Explore P01100 
Go to UniProtKB:  P01100
PHAROS:  P01100
GTEx:  ENSG00000170345 
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UniProt GroupP01100
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
AP-1 FRAGMENT JUNE [auth J]56Homo sapiensMutation(s): 2 
UniProt & NIH Common Fund Data Resources
Find proteins for P05412 (Homo sapiens)
Explore P05412 
Go to UniProtKB:  P05412
PHAROS:  P05412
GTEx:  ENSG00000177606 
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UniProt GroupP05412
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  • Reference Sequence

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Entity ID: 1
MoleculeChains LengthOrganismImage
DNA (5'-D(*DTP*DTP*DGP*DGP*DAP*DAP*DAP*DAP*DTP*DTP*DTP*DGP*DTP*DTP*DTP*DCP*DAP*DTP*DAP*DG)-3')20N/A
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  • Reference Sequence

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Entity ID: 2
MoleculeChains LengthOrganismImage
DNA (5'-D(*DAP*DAP*DCP*DTP*DAP*DTP*DGP*DAP*DAP*DAP*DCP*DAP*DAP*DAP*DTP*DTP*DTP*DTP*DCP*DC)-3')20N/A
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.303 
  • R-Value Work: 0.246 
  • R-Value Observed: 0.246 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 64.66α = 90
b = 85.46β = 112.03
c = 83.37γ = 90
Software Package:
Software NamePurpose
CCP4model building
X-PLORmodel building
X-PLORrefinement
DENZOdata reduction
SCALEPACKdata scaling
CCP4phasing
X-PLORphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-05-27
    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