Chen L, Glover J N, Hogan P G, Rao A, Harrison S C
Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
Nature. 1998 Mar 5;392(6671):42-8. doi: 10.1038/32100.
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.
活化T细胞核因子（NFAT）与AP-1异二聚体Fos-Jun协同结合一个复合DNA位点，并协同激活许多免疫反应基因的表达。NFAT、Fos和Jun的DNA结合结构域与包含白细胞介素-2基因启动子远端抗原受体反应元件的DNA片段形成的四聚体复合物的2.7埃分辨率晶体结构显示，在Fos和DNA弯曲的促进下，NFAT与AP-1之间存在一个延伸的界面。三种蛋白质在DNA上的紧密结合形成了一个连续的凹槽，用于识别15个碱基对。
