高等学校化学学报

高等学校化学学报 ›› 2009, Vol. 30 ›› Issue (11(1)): 9.

• 研究论文 • 上一篇    下一篇

生长素受体TIR1与四种生长素分子间相互作用的分子对接研究

贾雪冰, 王腾, 孙宏伟   

  1. 南开大学化学学院, 天津 300071
  • 收稿日期:2009-07-28 出版日期:2009-11-30 发布日期:2009-11-30
  • 通讯作者: 孙宏伟, 男, 博士, 教授, 主要从事分子模拟结构化学研究. E-mail: sunhw@nankai.edu.cn
  • 基金资助:

    国家高技术研究发展专项经费(批准号: 2006AA10A213)资助.

Docking to Explore the Interactions Between the Receptor TIR1 and Four Auxin Plant Hormones

JIA Xue-Bing, WANG Teng, SUN Hong-Wei*   

  1. College of Chemistry, Nankai University, Tianjin 300071, China
  • Received:2009-07-28 Online:2009-11-30 Published:2009-11-30
  • Contact: SUN Hong-Wei. E-mail: sunhw@nankai.edu.cn
  • Supported by:

    国家高技术研究发展专项经费(批准号: 2006AA10A213)资助.

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摘要：

依据生长素分子的分类以及生长素活性的不同, 选取四种生长素分子IAA, 1-NAA, 2,4-D, 2-NAA分别与生长素受体分子进行分子对接计算研究. 对生长素受体分子进行逐级对接计算. 首先, 通过分子对接计算研究辅酶InsP6以及中心水分子在生长素反应中的重要作用; 其次, 比较受体大分子完全刚性以及活性残基部分柔性的两种情况下的分子对接结果, 说明AutoDock4实现了受体分子活性残基的部分柔性而使对接结果更加合理, 进而使用AutoDock4方法对TIR1-Auxins体系进行对接计算; 最后, 对TIR1-Auxins-Aux/IAA体系进行分子对接计算, 结果表明, 生长素配体分子作为“分子胶水”直接与受体大分子TIR1以及底物多肽Aux/IAA形成强的弱相互作用, 如氢键作用、疏水相互作用, 促进了受体TIR1与Aux/IAA底物之间的结合, 进而说明氢键作用和疏水相互作用等弱相互作用对于生长素分子的活性具有很大的影响.

关键词: 分子对接; 生长素; F-盒式蛋白质TIR1; 氢键作用; 疏水相互作用

Abstract:

In this study, according to the classification and activity of auxin plant hormones the authors carry out docking experiments with four auxins, IAA, 1-NAA, 2,4-D, 2-NAA, and the receptor. The docking experiments are implemented step by step. First, the significant of co-factor InsP6 and center water in the mechanism of auxins are explored by docking; second, the experiments that compared with the docking rusults of two situations involving fully rigid and selective flexible of active residue of the receptor TIR1 illuminate that selective flexibility docking by AutoDock4 reports more rational results, so that, AutoDock4 dockings are implemented with TIR1-Auxins; third, AutoDock4 docking by TIR1-Auxins-Aux/IAA illuminates that auxin as a molecular glue enhances the interaction between TIR1 receptor and Aux/IAA substrate by the weak interactions, such as hydrogen bond and hydrophobic interaction, furthermore, the weak interactions between receptor protein and ligands greatly influence on auxin activity of auxin ligands.

Key words: Docking; Auxin; F-box protein TIR1; Hydrogen bond; Hydrophobic interaction

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