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Nature. 1998 Mar 5;392(6671):42-8.

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

Author information

1
Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, USA. lchen@xta1200.harvard.edu

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-A-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.

PMID:
9510247
DOI:
10.1038/32100
[Indexed for MEDLINE]

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