Study on the Structural Flexibility of Cysteine Protease TsCL-1 from Cysticercus Cellulose

›› 2017, Vol. 2 ›› Issue (6): 55-58.

Study on the Structural Flexibility of Cysteine Protease TsCL-1 from Cysticercus Cellulose

（1. School of Basic Medical Sciences, Wuhan University, Wuhan 430071, China; 2. Dali Institute of Schistosomiasis Prevention and Control, Dali, Yunnan 671000, China; 3. College of Agriculture and Biological Science, Dali University, Dali, Yunnan 671003, China）

Received:2016-12-07 Online:2017-06-15 Published:2017-06-15

Abstract

Abstract: Using the Molecular Dynamics Simulation method, the dynamic structural stability and conformational flexibility of cysteine protease TsCL-1 from Cysticercus cellulose have been investigated. The results indicate that TsCL- 1 contains an overall structural stability during the simulation. The results also indicate that the structural core of TsCL- 1 shows a small fluctuation amplitude, whereas most of the surface- exposed loops and the substrate binding sites experience significant conformational fluctuations and exhibit a highly structural flexibility. The results of this article will provide a solid basis for further studying the relationship between dynamic structural features and functions of TsCL-1.

Key words: Cysteine protease TsCL- 1, molecular dynamics simu?lations, dynamic structural flexibility, structure and function relationship

CLC Number:

Yang Lin, Zhu Yuexun, Yang Yanchao, Zhao Qinping, Yang Liquan. Study on the Structural Flexibility of Cysteine Protease TsCL-1 from Cysticercus Cellulose[J]. , 2017, 2(6): 55-58.

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