CRYSTAL-STRUCTURE OF TFIID TATA-BOX BINDING-PROTEIN
CRYSTAL-STRUCTURE OF TFIID TATA-BOX BINDING-PROTEIN
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DOI：
10.1038/360040a0
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发表时间：
1992-11-05
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;HU, SH;BURLEY, SK
真核生物转录器的核心组成部分，拟南芥的TATA盒结合蛋白（TBP或TFIIDtau）的结构已被确定的X射线晶体学在2.6埃分辨率。这种高度对称的α/β结构包含一个新的DNA结合折叠，类似于横跨DNA的分子“马鞍”。DNA结合表面是弯曲的、反平行的β-折叠。当与DNA结合时，鞍状物的凸面将呈现用于与其他转录起始因子和调节蛋白相互作用。
The structure of a central component of the eukaryotic transcriptional apparatus, a TATA-box binding protein (TBP or TFIIDtau) from Arabidopsis thaliana, has been determined by X-ray crystallography at 2.6 angstrom resolution. This highly symmetric alpha/beta structure contains a new DNA-binding fold, resembling a molecular 'saddle' that sits astride the DNA. The DNA-binding surface is a curved, antiparallel beta-sheet. When bound to DNA, the convex surface of the saddle would be presented for interaction with other transcription initiation factors and regulatory proteins.