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Solution structure of the core NFATC1/DNA complex

P Zhou1, L J Sun, V Dötsch

  • 1Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA.

Cell
|March 20, 1998
PubMed

Insights

The nuclear factor of activated T cells (NFAT) DNA-binding domain undergoes structural changes upon binding to DNA, facilitating gene regulation. This structural flexibility is key for protein interactions and gene transcription.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Immunology

Background:

  • Nuclear factor of the activated T cell (NFAT) transcription factors regulate cytokine gene expression.
  • NFAT proteins bind to promoter/enhancer regions of antigen-responsive genes, often with other DNA-binding partners.

Purpose of the Study:

  • To determine the solution structure of the binary complex between the human NFATC1 DNA-binding domain and the ARRE2 DNA site.
  • To understand how DNA binding influences NFAT structure and its role in transcriptional regulation.

Main Methods:

  • Solution structure determination of the NFATC1 DNA-binding domain/ARRE2 DNA complex.
  • Analysis of structural changes induced by DNA binding.

Main Results:

  • The structure of the binary NFATC1-DNA complex was elucidated.
  • DNA binding induces folding of key structural elements in NFATC1.
  • These elements are crucial for sequence-specific DNA recognition and protein-protein interactions.
  • The domain orientation in the binary complex differs from that in a ternary complex, suggesting conformational changes.

Conclusions:

  • DNA binding induces significant structural rearrangements in the NFAT DNA-binding domain.
  • These rearrangements are essential for NFAT function in gene regulation.
  • NFAT may reorient its DNA-binding domain upon forming cooperative transcriptional complexes.

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