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

Lin Chen (), J. N. Mark Glover, Patrick G. Hogan, Anjana Rao and Stephen C. Harrison ()
Additional contact information
Lin Chen: Department of Molecular and Cellular Biology
J. N. Mark Glover: Department of Molecular and Cellular Biology
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

Nature, 1998, vol. 392, issue 6671, 42-48

Abstract: 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.

Date: 1998
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DOI: 10.1038/32100

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