Crystal structure of triple-BRCT-domain of ECT2 and insights into the binding characteristics to CYK-4.

Abstract

Homo sapiens ECT2 is a cell cycle regulator that plays critical roles in cytokinesis. ECT2 activity is restrained during interphase via intra-molecular interactions that involve its N-terminal triple-BRCT-domain and its C-terminal DH-PH domain. At anaphase, this self-inhibitory mechanism is relieved by Plk1-phosphorylated CYK-4, which directly engages the ECT2 BRCT domain. To provide a structural perspective for this auto-inhibitory property, we solved the crystal structure of the ECT2 triple-BRCT-domain. In addition, we systematically analyzed the interaction between the ECT2 BRCT domains with phospho-peptides derived from its binding partner CYK-4, and have identified Ser164 as the major phospho-residue that links CYK-4 to the second ECT2 BRCT domain.

DOI: 10.1016/j.febslet.2014.07.019

Cite this paper

@article{Zou2014CrystalSO, title={Crystal structure of triple-BRCT-domain of ECT2 and insights into the binding characteristics to CYK-4.}, author={Yang Zou and Zhenhua Shao and Junhui Peng and Fudong Li and Deshun Gong and Chongyuan Wang and Xiaobing Zuo and Zhiyong Zhang and Jihui Wu and Yunyu Shi and Qingguo Gong}, journal={FEBS letters}, year={2014}, volume={588 17}, pages={2911-20} }