与DNA结合时Fli-1的ets结构域的溶液结构。

Solution structure of the ets domain of Fli-1 when bound to DNA.

作者信息

Liang H, Mao X, Olejniczak E T, Nettesheim D G, Yu L, Meadows R P, Thompson C B, Fesik S W

机构信息

Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, Illinois 60064, USA.

出版信息

Nat Struct Biol. 1994 Dec;1(12):871-5. doi: 10.1038/nsb1294-871.

DOI:10.1038/nsb1294-871

PMID:7773776

Abstract

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 alpha-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.

摘要

ets转录因子家族的成员共享一个保守的DNA结合结构域，即ets结构域。通过使用多维核磁共振技术，我们确定了人Fli-1的ets结构域与DNA结合形式的结构。它由三个α螺旋和一个四链β折叠组成，类似于最初在大肠杆菌的分解代谢物激活蛋白中发现的螺旋-转角-螺旋类DNA结合蛋白的结构。核磁共振和诱变实验表明，与结构相关的蛋白质相比，ets结构域使用了一种新的螺旋-转角-螺旋基序变体来结合DNA。