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Nature 392, 42-48 (5 March 1998) | doi:10.1038/32100; Received 17 September 1997; Accepted 23 December 1997

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

Lin Chen1, J. N. Mark Glover1,2, Patrick G. Hogan3, Anjana Rao3 & Stephen C. Harrison1,2

  1. Department of Molecular and Cellular Biology, Cambridge, Massachusetts 02138, USA
  2. Howard Hughes Medical Institute, Harvard University, Cambridge, Massachusetts 02138, USA
  3. Center for Blood Research, Harvard Medical School, Boston, Massachusetts 02115, USA

Correspondence to: Lin Chen1Stephen C. Harrison1,2 Correspondence and requests for materials should be addressed to S.C.H. or L.C. (e-mail: Email: schadmin@crystal.harvard.edu).Coordinates have been deposited at the Brookhaven Protein DataBank, accession code 1a02, and are also available bye-mail from lchen@xta 1200.harvard.edu.

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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.