高等学校化学学报

高等学校化学学报 ›› 2005, Vol. 26 ›› Issue (4): 689.

• 研究论文 • 上一篇    下一篇

细胞色素p450 2s1(CYP2s1)三维结构模建及其与维甲酸分子的对接研究

孙苗, 李泽生, 张媛, 郑清川, 孙家锺   

  1. 吉林大学理论化学研究所, 理论化学计算国家重点实验室, 长春 130023
  • 收稿日期:2004-10-09 出版日期:2005-04-10 发布日期:2005-04-10
  • 通讯作者: 李泽生(1954年出生),男,博士,博士生导师,从事理论化学基础理论及应用研究.E-mail:zeshengli@mai.ljlu.edu.cn E-mail:zeshengli@mai.ljlu.edu.cn
  • 基金资助:

    国家自然科学基金(批准号:20333050)资助.

Three Dimensional Homology Modeling of Cytochrome P450 2s1(CYP2s1) and Docking Study on CYP2s1-retinoid Acid

SUN Miao, LI Ze-Sheng, ZHANG Yuan, ZHENG Qing-Chuan, SUN Chia-Chung   

  1. Institute of Theoretical Chemistry, State Key Laboratory of Theoretical and Computational Chemistry, Jilin University, Changchun 130023, China
  • Received:2004-10-09 Online:2005-04-10 Published:2005-04-10

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被引次数

7

摘要： 利用同源模建和分子动力学模拟,模建了细胞色素P450(CYP2s1)的三维结构.在模建结构的基础上,分析了活性位点的组成和结构,并进行了与小分子(维甲酸)的分子对接研究.研究结果表明,在由维甲酸和CYP2s1形成的复合物中,非键相互作用较强,其中,GLu411和Ala414是与维甲酸相互作用能最强的两个残基,对复合物的结合起重要作用.

关键词: 同源模建, 细胞色素, 分子动力学

Abstract: By means of homology modeling and molecular dynamics simulation, the three dimensional (3D) structure of CYP2s1 was constructed on the basis of the crystal structure of CYP2c5 (PDB∶1DT6). The components and conformation of CYP2s1 binding site were proposed by using binding-site program and analyzing the binding site of the CYP family binding and catalysis characters. The ligand (retinoid acid) was docked to CYP2s1 by using the affinity program, and five conformations with lower energies were collected. By analyzing the complex of CYP2s1-retinoid acid which has the lowest energy among the five collected conformations, we know that nonbonding interaction is the major interaction in the complex, and the residues Glu 411 and Ala 414 play an important role in the binding and catalysis for this enzyme.

Key words: Homology modeling, Cytochrome, Molecular dynamics

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