Chem. J. Chinese Universities ›› 2010, Vol. 31 ›› Issue (4): 742.

• Articles • Previous Articles     Next Articles

Homology Model and Functional Prediction of the Three Dimensional Structure of HBsAg of Hepatitis Virus

ZHOU Xiao-Ping, ZHANG Mu-Xin, WANG Guang-Shu, YANG Xiao-Hong*   

  1. School of Pharmacy, Jilin University, Changchun 130021, China
  • Received:2009-04-25 Online:2010-04-10 Published:2010-04-10
  • Contact: YANG Xiao-Hong. E-mail: xiaohongyang88@126.com
  • Supported by:

    国家科技部支撑计划(批准号: 2006BAI06A18-19)资助.

Abstract:

When hepatitis B virus(HBV) conduct the planting process into normal liver cell, hepatitis B virus surface antigen(HBsAg) plays an important role during this process, but its crystal structure information has not been reported in the Protein Data Bank. In order to make further research about the structure and function of HBsAg, we constructed the three dimensional structure of HBsAg Pres12 using biology information homology model methods, and explored the mechanism as an important antiviral target at the molecular level by molecular simulation method. The results showed that the three dimensional structure of HBsAg consist the conformational Pres1 and the linear Pres2, three α-helixes and some loop region consist the whole structure, at the same time, some amino residues in the N-terminal of Pres1 make a cleft which forms the potential active site domain. The electrostatic analysis confirmed that, the N-terminal potential active site possess bigger electrostatic distribution and may have the ability to interact with recipient cell protein, this study will provide useful information for the design of anti-HBV drug molecules.

Key words: Hepatitis B; Surface antigen; Homology modeling; Molecular docking; Electro-static potential

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