Molecular docking of HSV-1 for identification of sulfolipid (SQDG) targeted protein
Issued Date
2010
Resource Type
Language
eng
Rights
Mahidol University
Bibliographic Citation
P.Kaewmanee,S.Hannongbua,P.Saparpakorn,K.Porkaew,V.Chumchua,N.Chirasuwan, et.al. Molecular docking of HSV-1 for identification of sulfolipid (SQDG) targeted protein. In: PACCON2010 (Pure and Applied Chemistry International Conference) p.165-168
Suggested Citation
P.Kaewmanee, S.Hannongbua, P.Saparpakorn, K.Porkaew, V.Chumchua, N.Chirasuwan, M.Ruengjitchatchawalya Molecular docking of HSV-1 for identification of sulfolipid (SQDG) targeted protein. P.Kaewmanee,S.Hannongbua,P.Saparpakorn,K.Porkaew,V.Chumchua,N.Chirasuwan, et.al. Molecular docking of HSV-1 for identification of sulfolipid (SQDG) targeted protein. In: PACCON2010 (Pure and Applied Chemistry International Conference) p.165-168. Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/43847
Title
Molecular docking of HSV-1 for identification of sulfolipid (SQDG) targeted protein
Other Contributor(s)
Abstract
The binding of non-ionic (L1) and ionic (1.2) forms of sulfo-quinovosyl-diacyf-glycerol (SQDG) structure, in three target protein structures
of Herpes Simplex Virus Type 1 (HSV-1), i.e. HSV-1 DNA polymerase (HSV-1 DNAPol); Glycoprotein D (gD); and Thymidine kinase (TK),were investigated
using GOLD programe.Results showed that both L1 and L2 posed the high fitness score with HSV-1 DNAPol chain B (46.49 and 44.49, respectively)
Amino acid containing positively charged sidechain, i.e. arginine (Arg), was found to be important in the binding to hydrophillic region of sulfonyl group,
while amino acid containing hydrophobic sidechain revealed the interaction to hydrophobic region, fatty acid chains, of the sulfolipid