高等学校化学学报 ›› 2009, Vol. 30 ›› Issue (7): 1423.

• 研究论文 • 上一篇    下一篇

新的α/β水解酶W14和W15的三维结构模建及分子对接研究

周奕含, 罗全, 韩葳葳, 姚远, 李泽生   

  1. 吉林大学理论化学研究所, 长春 130023
  • 收稿日期:2008-03-10 出版日期:2009-07-10 发布日期:2009-07-10
  • 通讯作者: 李泽生, 男, 博士, 教授, 博士生导师, 主要从事理论化学基础理论及应用研究. E-mail: zeshengli@mail.jlu.edu.cn
  • 基金资助:

    国家自然科学基金(批准号: 20333050, 20673044)资助.

Homology Modeling and Docking Studies of Novel α/β Hydrolase Fold Proteins W14 and W15

ZHOU Yi-Han, LUO Quan, HAN Wei-Wei, YAO Yuan, LI Ze-Sheng*   

  1. Institute of Theoretical Chemistry, Jilin University, Changchun 130023, China
  • Received:2008-03-10 Online:2009-07-10 Published:2009-07-10
  • Contact: LI Ze-Sheng. E-mail: zeshengli@mail.jlu.edu.cn
  • Supported by:

    国家自然科学基金(批准号: 20333050, 20673044)资助.

摘要:

利用同源模建和分子动力学模拟方法, 模建了两个新发现的α/β水解酶超家族成员W14和W15的三维结构, 并通过与α-醋酸萘酯的对接研究, 从理论上提出Gly82和Val13为形成“氧洞”的关键残基,有利于稳定水解过程中的带负电的过渡态, 以及其它对复合物形成起到重要作用的氨基酸残基.

关键词: 分子动力学; α/β水解酶; 分子对接

Abstract:

Three dimensional structure of novel α/β hydrolase fold proteins W14 and W15 were modeled by using homology and molecular dynamics methods. On the basis of the modeling, the components and the structures of active sites in W14 and W15 were analyzed and compared. The docking of 1-naphtyl acetate with the two proteins was also performed and compared. Gly82 and Val13 were key residues to form the oxyanion-hole and stabilized the negatively charged transition state that occurs during hydrolysis. Other important residues for binding were also identified.

Key words: Molecular dynamics; α/β Hydrolase; Molecular docking

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