1A66

SOLUTION NMR STRUCTURE OF THE CORE NFATC1/DNA COMPLEX, 18 STRUCTURES


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 18 
  • Conformers Submitted: 18 
  • Selection Criteria: NOE VIOLATION <= 0.4 ANGSTROM, DIHEDRAL ANGLE VIOLATION <= 5 DEGREE 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Solution structure of the core NFATC1/DNA complex.

Zhou, P.Sun, L.J.Dotsch, V.Wagner, G.Verdine, G.L.

(1998) Cell 92: 687-696

  • DOI: https://doi.org/10.1016/s0092-8674(00)81136-8
  • Primary Citation of Related Structures:  
    1A66

  • PubMed Abstract: 

    The nuclear factor of the activated T cell (NFAT) family of transcription factors regulates cytokine gene expression by binding to the promoter/enhancer regions of antigen-responsive genes, usually in cooperation with heterologous DNA-binding partners. Here we report the solution structure of the binary complex formed between the core DNA-binding domain of human NFATC1 and the ARRE2 DNA site from the interleukin-2 promoter. The structure reveals that DNA binding induces the folding of key structural elements that are required for both sequence-specific recognition and the establishment of cooperative protein-protein contacts. The orientation of the NFAT DNA-binding domain observed in the binary NFATC1-DBD*/ DNA complex is distinct from that seen in the ternary NFATC2/AP-1/DNA complex, suggesting that the domain reorients upon formation of a cooperative transcriptional complex.


  • Organizational Affiliation

    Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA.


Macromolecules

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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
CORE NFATC1C [auth A]178Homo sapiensMutation(s): 3 
Gene Names: NFATC1(416-591)
UniProt & NIH Common Fund Data Resources
Find proteins for O95644 (Homo sapiens)
Explore O95644 
Go to UniProtKB:  O95644
PHAROS:  O95644
GTEx:  ENSG00000131196 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO95644
Sequence Annotations
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  • Reference Sequence

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Entity ID: 1
MoleculeChains LengthOrganismImage
DNA (5'-D(*CP*GP*AP*GP*GP*AP*AP*AP*AP*TP*TP*G)-3')A [auth B]12N/A
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains LengthOrganismImage
DNA (5'-D(*CP*AP*AP*TP*TP*TP*TP*CP*CP*TP*CP*G)-3')B [auth C]12N/A
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 18 
  • Conformers Submitted: 18 
  • Selection Criteria: NOE VIOLATION <= 0.4 ANGSTROM, DIHEDRAL ANGLE VIOLATION <= 5 DEGREE 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-06-17
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2021-11-03
    Changes: Database references, Derived calculations, Other