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

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

  • FEBS Lett. 2014 Aug 25;588(17):2911-20. doi: 10.1016/j.febslet.2014.07.019.
Yang Zou 1 Zhenhua Shao 1 Junhui Peng 1 Fudong Li 1 Deshun Gong 1 Chongyuan Wang 1 Xiaobing Zuo 2 Zhiyong Zhang 1 Jihui Wu 1 Yunyu Shi 1 Qingguo Gong 3
Affiliations

Affiliations

  • 1 Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China.
  • 2 X-ray Science Division, Advanced Photon Source, Argonne National Laboratory, Argonne, IL 60349, USA.
  • 3 Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China. Electronic address: qgg@ustc.edu.cn.
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.

Keywords

Auto-inhibition; Binding pocket; Phospho-peptide; The epithelial cell transforming protein 2; Triple-BRCT-domain.

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