| First Author | Chen L | Year | 1998 |
| Journal | Nature | Volume | 392 |
| Issue | 6671 | Pages | 42-8 |
| PubMed ID | 9510247 | Mgi Jnum | J:319998 |
| Mgi Id | MGI:6867163 | Doi | 10.1038/32100 |
| Citation | Chen L, et al. (1998) Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA. Nature 392(6671):42-8 |
| abstractText | 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. |
