CRYSTAL-STRUCTURE OF TFIID TATA-BOX BINDING-PROTEIN

被引：358

作者：

NIKOLOV, DB

HU, SH

LIN, J

GASCH, A

HOFFMANN, A

HORIKOSHI, M

CHUA, NH

ROEDER, RG

BURLEY, SK

机构：

[1] ROCKEFELLER UNIV,MOLEC BIOPHYS LABS,1230 YORK AVE,NEW YORK,NY 10021

[2] ROCKEFELLER UNIV,PLANT MOLEC BIOL LAB,NEW YORK,NY 10021

[3] ROCKEFELLER UNIV,BIOCHEM & MOLEC BIOL LAB,NEW YORK,NY 10021

[4] ROCKEFELLER UNIV,HOWARD HUGHES MED INST,NEW YORK,NY 10021

来源：

NATURE | 1992年 / 360卷 / 6399期

关键词：

D O I：

10.1038/360040a0

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 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.

引用

页码：40 / 46

页数：7

共 67 条

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