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[1]陈秀博,晋文燕,吴晓辉,等.CDC25B与CDK2/Cyclin A蛋白相互作用研究[J].天津医科大学学报,2018,24(03):197-200,204.
　CHEN Xiu-bo,JIN Wen-yan,WU Xiao-hui,et al.Study on the interaction between CDC25B and CDK2/Cyclin A[J].Journal of Tianjin Medical University,2018,24(03):197-200,204.
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《天津医科大学学报》[ISSN:1006-8147/CN:12-1259/R]

卷:
24卷
期数:
2018年03期
页码:
197-200,204
栏目:
出版日期:
2018-05-20

文章信息/Info

Title:
Study on the interaction between CDC25B and CDK2/Cyclin A
作者:
陈秀博; 晋文燕; 吴晓辉; 马英
天津医科大学药学院，天津市临床药物关键技术重点实验室，天津300070
Author(s):
CHEN Xiu-bo;  JIN Wen-yan;  WU Xiao-hui;  MA-Ying
School of Pharmacy, Tianjin Medical University, Tianjin Key Laboratory on Technologies Enabling Development of Clinical Therapeutics and Diagnostics, Tianjin 300070, China
关键词:
CDC25B; CDK2/Cyclin A; 蛋白-蛋白对接; 关键氨基酸
Keywords:
CDC25B;  CDK2/Cyclin A;  protein-protein docking;  key residues
分类号:
R914.2
DOI:
-
文献标志码:
A
摘要:
目的：研究双特异性蛋白磷酸酶B（CDC25B）与细胞周期素 A(Cyclin A)和细胞周期素依赖性激酶2（CDK2）蛋白发生相互作用的结构基础。方法：应用Discovery Studio (DS) v3.5中的ZDOCK模块对CDC25B与CDK2/Cyclin A蛋白进行对接。应用“Analyze Protein Interface”模块计算CDC25B蛋白和CDK2/Cyclin A蛋白的溶剂可及表面积（SAS）并分析CDC25B蛋白和CDK2/Cyclin A蛋白相互作用界面的关键氨基酸残基。应用“Calculate Interaction Energy”模块计算 CDC25B蛋白和CDK2/Cyclin A蛋白相互作用界面处的关键氨基酸残基间的相互作用能。结果：对pose 1的疏水相互作用、氢键相互作用、相互作用能进行计算分析，预测得到CDC25B-CDK2/Cyclin A复合物的结合模式及起相互作用的氨基酸残基（CDC25B: GLY380，TYR382， ARG485, ARG488，GLU489，ARG490，ARG492，TYR497；CDK2/Cyclin A：THR165, TRP167，ASP206，SER207，ASP210, PHE213）。结论：该结果为今后深入研究 CDC25B通路和发挥协同刺激作用的信号体系以及基于该信号途径新型分子靶向药物的设计提供了理论基础。
Abstract:
Objective: To explore the protein-protein interactions between the cell division cyclin 25 B (CDC25B) and Cyclin A and cyclin-dependent kinase 2(CDK2). Methods: The docking analysis of CDC25B andCDK2/Cyclin A was performed using the protein-protein docking algorithm ZDOCK embed in Discovery Studio(DS) v3.5 and the theoretical binding domain between them was predicted. The SAS and the interface of CDC25B and CDK2/Cyclin A were calculated by the “Analyze Protein Interface” algorithm. The key residues and the interaction energy of the interface of the two proteins were also calculated by the “Calculate Interaction Energy”. Results: Protein-protein interaction analysis of pose1 including hydrophobic interaction, H-bond interaction and interaction energy discovered the binding model of CDC25B and CDK2/Cyclin A and the key residues played an important role in stabilizing the complex(CDC25B: GLY380, TYR382, ARG485, ARG488, GLU489, ARG490, ARG492, and TYR497; CDK2/Cyclin A: THR165, TRP167, ASP206, SER207, ASP210, PHE213). Conclusion: The data presented in the paper are essential not only for the in-depth study of the co-stimulatory signaling mechanism of CDC25B pathway but also for the development of cancer therapeutics targeting CDC25B.

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备注/Memo

备注/Memo:
文章编号 1006-8147(2018)03-0197-04
基金项目 天津市自然科学基金重点项目基金资助（16JCZDJC32500）
作者简介 陈秀博(1990-)，男，硕士在读，研究方向：临床药理学；通信作者：马英，E-mail: maying@tmu.edu.cn 。
更新日期/Last Update: 2018-05-20