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

被引:423
作者
Chen, L
Glover, JNM
Hogan, PG
Rao, A
Harrison, SC [1 ]
机构
[1] Harvard Univ, Dept Mol & Cellular Biol, Cambridge, MA 02138 USA
[2] Harvard Univ, Howard Hughes Med Inst, Cambridge, MA 02138 USA
[3] Harvard Univ, Sch Med, Ctr Blood Res, Boston, MA 02115 USA
关键词
D O I
10.1038/32100
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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-Angstrom-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.
引用
收藏
页码:42 / 48
页数:7
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