4N40

Crystal structure of human Epithelial cell-transforming sequence 2 protein

Summary for 4N40

• Entry DOI: 10.2210/pdb4n40/pdb
• Descriptor: Protein ECT2 (1 entity in total)
• Functional Keywords: triple brct domains, cell cycle
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q9H8V3
• Total number of polymer chains: 1
• Total formula weight: 33073.29

Authors

Zou, Y.,Shao, Z.H.,Li, F.D.,Gong, D.,Wang, C.,Gong, Q.,Shi, Y. (deposition date: 2013-10-08, release date: 2014-08-27, Last modification date: 2024-10-09)

Primary citation

Zou, Y.,Shao, Z.H.,Peng, J.,Li, F.D.,Gong, D.,Wang, C.,Zuo, X.,Zhang, Z.,Wu, J.,Shi, Y.,Gong, Q.
Crystal structure of triple-BRCT-domain of ECT2 and insights into the binding characteristics to CYK-4
Febs Lett., 588:2911-2920, 2014

PubMed 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.

PubMed: 25068414
DOI: 10.1016/j.febslet.2014.07.019

Experimental method

X-RAY DIFFRACTION (3.106 Å)