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

Author

Listed:
  • Lin Chen

    (Department of Molecular and Cellular Biology)

  • J. N. Mark Glover

    (Department of Molecular and Cellular Biology
    Howard Hughes Medical Institute, Harvard University)

  • Patrick G. Hogan

    (Center for Blood Research, Harvard Medical School)

  • Anjana Rao

    (Center for Blood Research, Harvard Medical School)

  • Stephen C. Harrison

    (Department of Molecular and Cellular Biology
    Howard Hughes Medical Institute, Harvard University)

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-Å-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.

Suggested Citation

  • Lin Chen & J. N. Mark Glover & Patrick G. Hogan & Anjana Rao & Stephen C. Harrison, 1998. "Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA," Nature, Nature, vol. 392(6671), pages 42-48, March.
    • Handle: RePEc:nat:nature:v:392:y:1998:i:6671:d:10.1038_32100
    DOI: 10.1038/32100
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    Cited by:

    1. Nikolai Schleussner & Pierre Cauchy & Vedran Franke & Maciej Giefing & Oriol Fornes & Naveen Vankadari & Salam A. Assi & Mariantonia Costanza & Marc A. Weniger & Altuna Akalin & Ioannis Anagnostopoulo, 2023. "Transcriptional reprogramming by mutated IRF4 in lymphoma," Nature Communications, Nature, vol. 14(1), pages 1-18, December.

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