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Nonsubstrate Based Inhibitors of Dengue Virus Serine Protease: A Molecular Docking Approach to Study Binding Interactions between Protease and Inhibitors

Lee, Y.K., and Tan, S.K., and Habibah Abdul Wahab, and Rohana Yusof, and Noorsaadah Abd. Rahman, (2007) Nonsubstrate Based Inhibitors of Dengue Virus Serine Protease: A Molecular Docking Approach to Study Binding Interactions between Protease and Inhibitors. Asia Pacific Journal of Molecular Biology & Biotechnology, 15 (2). pp. 53-59.

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Affiliations

University of Malaya. Faculty of Science. Dept. of Chemistry
University of Malaya. Faculty of Science. Institute of Biological Sciences
Universiti Sains Malaysia. School of Pharmacy
University of Malaya. Dept. of Mol. Medicine
University of Malaya. Faculty of Science. Dept. of Chemistry

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.

Item Type:Journal
Additional Information:The authors acknowledge financial support for this project provided by the Malaysian Ministry of Science, Technology and Innovation under the Top Down National Biotechnology Directory grant no 09-02-04-001BTK/TH/004 (UM 36-02-03-6008) and the Malaysian Academy of Science SAGA funds.
Keywords:Dengue virus, serine protease, NS2B/NS3 complex, ligand docking
Subjects:Q Science, Computer Science
ID Code:3764

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