Nikolov D B, Chen H, Halay E D, Usheva A A, Hisatake K, Lee D K, Roeder R G, Burley S K
Laboratories of Molecular Biophysics, Rockefeller University, New York, New York 10021, USA.
Nature. 1995 Sep 14;377(6545):119-28. doi: 10.1038/377119a0.
The crystal structure of the transcription factor IIB (TFIIB)/TATA box-binding protein (TBP)/TATA-element ternary complex is described at 2.7 A resolution. Core TFIIB resembles cyclin A, and recognizes the preformed TBP-DNA complex through protein-protein and protein-DNA interactions. The amino-terminal domain of core TFIIB forms the downstream surface of the ternary complex, where it could fix the transcription start site. The remaining surfaces of TBP and the TFIIB can interact with TBP-associated factors, other class II initiation factors, and transcriptional activators and coactivators.
转录因子IIB（TFIIB）/TATA盒结合蛋白（TBP）/TATA元件三元复合物的晶体结构在2.7埃分辨率下得以描述。核心TFIIB类似于细胞周期蛋白A，并通过蛋白质-蛋白质和蛋白质-DNA相互作用识别预先形成的TBP-DNA复合物。核心TFIIB的氨基末端结构域形成三元复合物的下游表面，在此处它可以确定转录起始位点。TBP和TFIIB的其余表面可以与TBP相关因子、其他II类起始因子以及转录激活因子和共激活因子相互作用。
