Crystal structure of triple‐BRCT‐domain of ECT2 and insights into the binding characteristics to CYK‐4
Copyright policy )Crystal structure of triple‐BRCT‐domain of ECT2 and insights into the binding characteristics to CYK‐4
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.
- University of Science and Technology of China China (People's Republic of)
- Argonne National Laboratory United States
Binding pocket, GTPase-Activating Proteins, Molecular Sequence Data, Phospho-peptide, The epithelial cell transforming protein 2, Triple-BRCT-domain, Molecular Dynamics Simulation, Crystallography, X-Ray, Protein Structure, Tertiary, Mice, Phosphoserine, Auto-inhibition, Proto-Oncogene Proteins, Animals, Humans, Cattle, Amino Acid Sequence, Phosphorylation, Protein Binding
Binding pocket, GTPase-Activating Proteins, Molecular Sequence Data, Phospho-peptide, The epithelial cell transforming protein 2, Triple-BRCT-domain, Molecular Dynamics Simulation, Crystallography, X-Ray, Protein Structure, Tertiary, Mice, Phosphoserine, Auto-inhibition, Proto-Oncogene Proteins, Animals, Humans, Cattle, Amino Acid Sequence, Phosphorylation, Protein Binding
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