2. Academic Validation
  3. 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.
PMID: 25068414 DOI: 10.1016/j.febslet.2014.07.019
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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