Publication Abstract from PubMed
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.
Crystal structure of triple-BRCT-domain of ECT2 and insights into the binding characteristics to CYK-4.,Zou Y, Shao Z, Peng J, Li F, Gong D, Wang C, Zuo X, Zhang Z, Wu J, Shi Y, Gong Q FEBS Lett. 2014 Aug 25;588(17):2911-20. doi: 10.1016/j.febslet.2014.07.019. Epub , 2014 Jul 25. PMID:25068414[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
