Summary information and primary citation
- PDB-id
- 1a02; SNAP-derived features in text and JSON formats;
DNAproDB
- 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.
