SOLUTION STRUCTURE OF THE ETS DOMAIN OF FLI-1 WHEN BOUND TO DNA

被引：96

作者：

LIANG, H

MAO, XH

OLEJNICZAK, ET

NETTESHEIM, DG

YU, LP

MEADOWS, RP

THOMPSON, CB

FESIK, SW

机构：

[1] ABBOTT LABS,DIV PHARMACEUT DISCOVERY,ABBOTT PK,IL 60064

[2] UNIV CHICAGO,HOWARD HUGHES MED INST,CHICAGO,IL 60637

[3] UNIV CHICAGO,DEPT MOLEC GENET & CELL BIOL,CHICAGO,IL 60637

来源：

NATURE STRUCTURAL BIOLOGY | 1994年 / 1卷 / 12期

关键词：

D O I：

10.1038/nsb1294-871

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Members of the ets family of transcription factors share a conserved DNA-binding domain, the ets domain. By using multidimensional NMR we have determined the structure of the ets domain of human Fli-1 in the DNA-bound form. It consists of three a-helices and a four-stranded beta-sheet, similar to structures of the class of helix-turn-helix DNA binding proteins first found in the catabolite activator protein of Escherichia coli. NMR and mutagenesis experiments suggest that in comparison to structurally related proteins, the ets domain uses a new variation of the helix-turn-helix motif for binding to DNA.

引用

页码：871 / 876

页数：6

共 46 条

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