Kodandapani R, Pio F, Ni C Z, Piccialli G, Klemsz M, McKercher S, Maki R A, Ely K R
La Jolla Cancer Research Center at the Burnham Institute, California 92037, USA.
Nature. 1996 Apr 4;380(6573):456-60. doi: 10.1038/380456a0.
The Ets family of transcription factors, of which there are now about 35 members regulate gene expression during growth and development. They share a conserved domain of around 85 amino acids which binds as a monomer to the DNA sequence 5'-C/AGGAA/T-3'. We have determined the crystal structure of an ETS domain complexed with DNA, at 2.3-A resolution. The domain is similar to alpha + beta (winged) 'helix-turn-helix' proteins and interacts with a ten-base-pair region of duplex DNA which takes up a uniform curve of 8 degrees. The domain contacts the DNA by a novel loop-helix-loop architecture. Four of amino acids that directly interact with the DNA are highly conserved: two arginines from the recognition helix lying in the major groove, one lysine from the 'wing' that binds upstream of the core GGAA sequence, and another lysine, from the 'turn' of the 'helix-turn-helix' motif, which binds downstream and on the opposite strand.
Ets转录因子家族目前约有35个成员，在生长和发育过程中调节基因表达。它们共享一个约85个氨基酸的保守结构域，该结构域作为单体与DNA序列5'-C/AGGAA/T-3'结合。我们已确定了与DNA复合的ETS结构域的晶体结构，分辨率为2.3埃。该结构域类似于α + β（带翼）“螺旋-转角-螺旋”蛋白，并与双链DNA的一个十碱基对区域相互作用，该区域呈现8度的均匀弯曲。该结构域通过一种新颖的环-螺旋-环结构与DNA接触。与DNA直接相互作用的四个氨基酸高度保守：来自识别螺旋的两个精氨酸位于大沟中，来自“翼”的一个赖氨酸结合在核心GGAA序列的上游，以及来自“螺旋-转角-螺旋”基序“转角”的另一个赖氨酸，它结合在下游且位于相反链上。
