Integrated in silico-in vitro characterization, identification and disruption of the intermolecular interaction between SH3 domain-containing protein kinases and human pituitary tumor-transforming gene 1

• Published in: General physiology and biophysics Vol. 36; no. 1; p. 91
• Main Authors: Li, Yanan, Li, Mengmeng, Min, Weijie, Han, Guosheng, Wang, Laixing, Chen, Chao, Li, Zifu, Zhang, Yuhui, Li, Jianmin, Yue, Zhijian
• Format: Journal Article
• Language: English
• Published: Slovakia 01.01.2017
• Subjects: Binding Sites; Enzyme Activation; Humans; MAP Kinase Kinase Kinases - chemistry; MAP Kinase Kinase Kinases - ultrastructure; Models, Chemical; Molecular Docking Simulation; Phosphatidylinositol 3-Kinases - chemistry; Phosphatidylinositol 3-Kinases - ultrastructure; Protein Binding; Protein Conformation; Securin - chemistry; Securin - ultrastructure; src Homology Domains; Structure-Activity Relationship; Substrate Specificity

The human pituitary tumor-transforming gene-1 (hPTTG1) has been found to be overexpressed in various cancers. Accumulated evidences implicate that some of protein kinases can specifically recognize two PXXP motifs at hPTTG1 C-terminus through their Src homology (SH3) domain and then phosphorylate th...