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Title: Nonsubstrate Based Inhibitors of Dengue Virus Serine Protease: A Molecular Docking Approach to Study Binding Interactions between Protease and Inhibitors
Authors: Kee, L.Y. 
Kiat, T.S. 
Wahab, H.A. 
Yusof, R. 
Rahman, N.A. 
Issue Date: 2007
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.
Appears in Collections:COE Scholarly Publication

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