Please use this identifier to cite or link to this item:
http://dspace.uniten.edu.my/jspui/handle/123456789/9827
DC Field | Value | Language |
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dc.contributor.author | Kee, L.Y. | |
dc.contributor.author | Kiat, T.S. | |
dc.contributor.author | Wahab, H.A. | |
dc.contributor.author | Yusof, R. | |
dc.contributor.author | Rahman, N.A. | |
dc.date.accessioned | 2018-03-06T03:50:12Z | - |
dc.date.available | 2018-03-06T03:50:12Z | - |
dc.date.issued | 2007 | |
dc.identifier.uri | http://dspace.uniten.edu.my/jspui/handle/123456789/9827 | - |
dc.description.abstract | The protein-ligand binding interactions studies were carried out by performing dockings of the ligands that were found to be competitively inhibiting the activities of the DEN2 NS2B/NS3 serine protease onto the catalytic triad of a model of DEN2 NS2B/NS3 protease. Results indicate the importance of three out of the five residues reported to be essential for binding activities of the NS2B/NS3 serine protease. These residues are Tyr-150, Asn-152 and Gly-153. In addition, Ser-135 and Gly-151 were also found to be very important in forming hydrogen bonds with the inhibitors. Moreover, Ser-131, Pro-132, Tyr-150 and Asn-152 were found to be important for van der Waals interaction of the ligand, while Val-52, Leu-128, Pro-132 and Val-155 are involved in hydrophobic interaction with the inhibitors. | |
dc.title | Nonsubstrate Based Inhibitors of Dengue Virus Serine Protease: A Molecular Docking Approach to Study Binding Interactions between Protease and Inhibitors | |
item.fulltext | No Fulltext | - |
item.grantfulltext | none | - |
crisitem.author.dept | Universiti Tenaga Nasional | - |
Appears in Collections: | COE Scholarly Publication |
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