CRYSTAL-STRUCTURE OF A TFIIB-TBP-TATA-ELEMENT TERNARY COMPLEX
CRYSTAL-STRUCTURE OF A TFIIB-TBP-TATA-ELEMENT TERNARY COMPLEX
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DOI：
10.1038/377119a0
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发表时间：
1995-09-14
期刊：
影响因子：
64.8
通讯作者：
BURLEY, SK
中科院分区：
文献类型：
--
作者：
NIKOLOV, DB;CHEN, H;BURLEY, SK
转录因子IIB(TFIIB)/TATA盒结合蛋白(TBP)/TATA元件三元复合体的晶体结构以2.7埃分辨率描述，核心TFIIB类似于细胞周期蛋白A，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复合体。核心TFIIB的氨基末端结构域形成三元复合体的下游表面，在那里它可以固定转录起始点。TBP和TFIIB的其余表面可以与TBP相关因子、其他II类启动因子以及转录激活因子和辅助激活因子相互作用。
The crystal structure of the transcription factor IIB (TFIIB)/TATA box-binding protein (TBP)/TATA-element ternary complex is described at 2.7 Angstrom 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.