Chem. J. Chinese Universities ›› 2009, Vol. 30 ›› Issue (7): 1423.

• Articles • Previous Articles     Next Articles

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.

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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