Summary information and primary citation
- PDB-id
-
1a02;
SNAP-derived features in text and
JSON formats
- Class
- transcription-DNA
- Method
- X-ray (2.7 Å)
- Summary
- Structure of the DNA binding domains of nfat, fos and
jun bound to DNA
- Reference
-
Chen L, Glover JN, Hogan PG, Rao A, Harrison SC (1998):
"Structure
of the DNA-binding domains from NFAT, Fos and Jun bound
specifically to DNA." Nature,
392, 42-48. doi: 10.1038/32100.
- 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.