Acta Phys. -Chim. Sin. ›› 2009, Vol. 25 ›› Issue (03): 417-422.doi: 10.3866/PKU.WHXB20090304

• ARTICLE • Previous Articles     Next Articles

Homology Modeling of Human Serine Racemase and Its Molecular Docking with Peptide Inhibitors

ZHAO Yong-Shan, ZHENG Qing-Chuan, ZHANG Hong-Xing, CHU Hui-Ying, SUN Chia-Chung   

  1. State Key Laboratory of Theoretical and Computational Chemistry, Institute of Theoretical Chemistry, Jilin University, Changchun 130023, P. R. China
  • Received:2008-11-04 Revised:2008-12-11 Published:2009-03-02
  • Contact: ZHENG Qing-Chuan E-mail:zhengqch@jlu.edu.cn

Abstract:

The three dimensional structure of human serine racemase (hSR) was modeled and refined using homology modeling and molecular dynamics simulation. This model was assessed by profile-3D and procheck, which confirmed that the refined model was reliable. Complex structures of peptide inhibitors with hSR were obtained and investigated through ligand-receptor docking studies by a molecular docking program, affinity. The binding pattern predicted by the affinity module revealed that important residues interacted with the peptide inhibitors and the module provided further refinement of the hSR/inhibitor binding interaction that may be used as a basis for new structure-based design efforts.

Key words: Human serine racemase, Molecular dynamics simulation, Molecular docking, Homology modeling

MSC2000: 

  • O641