4N40

Crystal structure of human Epithelial cell-transforming sequence 2 protein

4N40 の概要

• エントリーDOI: 10.2210/pdb4n40/pdb
• 分子名称: Protein ECT2 (1 entity in total)
• 機能のキーワード: triple brct domains, cell cycle
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q9H8V3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33073.29

構造登録者

Zou, Y.,Shao, Z.H.,Li, F.D.,Gong, D.,Wang, C.,Gong, Q.,Shi, Y. (登録日: 2013-10-08, 公開日: 2014-08-27, 最終更新日: 2024-10-09)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.106 Å)