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Crystal structure of triple-BRCT-domain of ECT2 and insights into the binding characteristics to CYK-4
- Zou, Yang, Shao, Zhenhua, Peng, Junhui, Li, Fudong, Gong, Deshun, Wang, Chongyuan, Zuo, Xiaobing, Zhang, Zhiyong, Wu, Jihui, Shi, Yunyu, Gong, Qingguo
- FEBS letters 2014 v.588 pp. 2911-2920
- Homo sapiens, anaphase, binding properties, crystal structure, cytokinesis, interphase
- 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.