Nonsubstrate based inhibitors of dengue virus serine protease: a molecular docking approach to study binding interactions between protease and inhibitors
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...
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| Format: | Article |
| Language: | English |
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Malaysian Society for Molecular Biology and Biotechnology
2007
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| Online Access: | http://eprints.um.edu.my/7137/1/Non-substrate_Based_Inhibitors_of_Dengue_Virus_Serine_Protease.pdf |
| _version_ | 1796945532172632064 |
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| author | Lee, Y.K. Tan, S.K. Wahab, H.A. Yusof, Rohana Abd Rahman, N. |
| author_facet | Lee, Y.K. Tan, S.K. Wahab, H.A. Yusof, Rohana Abd Rahman, N. |
| author_sort | Lee, Y.K. |
| collection | UM |
| description | 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. |
| first_indexed | 2024-03-06T05:18:06Z |
| format | Article |
| id | um.eprints-7137 |
| institution | Universiti Malaya |
| language | English |
| last_indexed | 2024-03-06T05:18:06Z |
| publishDate | 2007 |
| publisher | Malaysian Society for Molecular Biology and Biotechnology |
| record_format | dspace |
| spelling | um.eprints-71372021-04-28T07:23:05Z http://eprints.um.edu.my/7137/ Nonsubstrate based inhibitors of dengue virus serine protease: a molecular docking approach to study binding interactions between protease and inhibitors Lee, Y.K. Tan, S.K. Wahab, H.A. Yusof, Rohana Abd Rahman, N. R Medicine 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. Malaysian Society for Molecular Biology and Biotechnology 2007 Article PeerReviewed application/pdf en http://eprints.um.edu.my/7137/1/Non-substrate_Based_Inhibitors_of_Dengue_Virus_Serine_Protease.pdf Lee, Y.K. and Tan, S.K. and Wahab, H.A. and Yusof, Rohana and Abd Rahman, N. (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 and Biotechnology, 15 (2). pp. 53-59. ISSN 0128-7451, |
| spellingShingle | R Medicine Lee, Y.K. Tan, S.K. Wahab, H.A. Yusof, Rohana Abd Rahman, N. Nonsubstrate based inhibitors of dengue virus serine protease: a molecular docking approach to study binding interactions between protease and inhibitors |
| title | Nonsubstrate based inhibitors of dengue virus serine protease: a molecular docking approach to study binding interactions between protease and inhibitors |
| title_full | Nonsubstrate based inhibitors of dengue virus serine protease: a molecular docking approach to study binding interactions between protease and inhibitors |
| title_fullStr | Nonsubstrate based inhibitors of dengue virus serine protease: a molecular docking approach to study binding interactions between protease and inhibitors |
| title_full_unstemmed | Nonsubstrate based inhibitors of dengue virus serine protease: a molecular docking approach to study binding interactions between protease and inhibitors |
| title_short | Nonsubstrate based inhibitors of dengue virus serine protease: a molecular docking approach to study binding interactions between protease and inhibitors |
| title_sort | nonsubstrate based inhibitors of dengue virus serine protease a molecular docking approach to study binding interactions between protease and inhibitors |
| topic | R Medicine |
| url | http://eprints.um.edu.my/7137/1/Non-substrate_Based_Inhibitors_of_Dengue_Virus_Serine_Protease.pdf |
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