SECONDARY STRUCTURE OF THE ETS DOMAIN PLACES MURINE ETS-1 IN THE SUPERFAMILY OF WINGED HELIX-TURN-HELIX DNA-BINDING PROTEINS
SECONDARY STRUCTURE OF THE ETS DOMAIN PLACES MURINE ETS-1 IN THE SUPERFAMILY OF WINGED HELIX-TURN-HELIX DNA-BINDING PROTEINS
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DOI：
10.1021/bi00250a001
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发表时间：
1994-11-22
期刊：
影响因子：
2.9
通讯作者：
MCINTOSH, LP
中科院分区：
文献类型：
--
作者：
DONALDSON, LW;PETERSEN, JM;MCINTOSH, LP
转录因子的ets基因家族的成员的特征在于保守的85个残基的DNA结合区域，称为ETS结构域，其与结构上表征的DNA结合基序缺乏序列同源性。小鼠ETS-1的ETS结构域的二级结构的基础上确定的NMR化学位移，NOE和J-耦合的限制，酰胺氢交换，圆二色性，和FT-IR光谱。ETS结构域由以H1-S1-S2-H2-H3-S3-S4顺序排列的三个α-螺旋（H）和四个β-链（S）组成。四链反平行β折叠是由螺旋2和3形成的推定螺旋-转角-螺旋DNA识别基序的支架。延伸超出ETS结构域至截短的Ets-1的天然C-末端的25个残基也含有螺旋片段。基于这种拓扑结构与分解代谢物激活蛋白（CAP）、热休克因子（HSF）和肝细胞核因子（HNF-3 γ）的相似性，我们提出ets蛋白是有翼螺旋-转角-螺旋DNA结合蛋白超家族的成员。
The members of the ets gene family of transcription factors are characterized by a conserved 85-residue DNA-binding region, termed the ETS domain, that lacks sequence homology to structurally characterized DNA-binding motifs. The secondary structure of the ETS domain of murine Ets-1 was determined on the basis of NMR chemical shifts, NOE and J-coupling constraints, amide hydrogen exchange, circular dichroism, and FT-IR spectroscopy. The ETS domain is composed of three a-helices (H) and four beta-strands (S) arranged in the order H1-S1-S2-H2-H3-S3-S4. The four-stranded antiparallel beta-sheet is the scaffold for a putative helix-turn-helix DNA recognition motif formed by helices 2 and 3. The 25 residues extending beyond the ETS domain to the native C-terminus of the truncated Ets-1 also contain a helical segment. On the basis of the similarity of this topology with that of catabolite activator protein (CAP), heat shock factor (HSF), and hepatocyte nuclear factor (HNF-3 gamma), we propose that ets proteins are members of the superfamily of winged helix-turn-helix DNA-binding proteins.