Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus
Top Cited Papers
- 12 March 2006
- journal article
- research article
- Published by Springer Science and Business Media LLC in Nature Structural & Molecular Biology
- Vol. 13 (4), 372-373
- https://doi.org/10.1038/nsmb1073
Abstract
The replication of flaviviruses requires the correct processing of their polyprotein by the viral NS3 protease (NS3pro). Essential for the activation of NS3pro is a 47-residue region of NS2B. Here we report the crystal structures of a dengue NS2B–NS3pro complex and a West Nile virus NS2B–NS3pro complex with a substrate-based inhibitor. These structures identify key residues for NS3pro substrate recognition and clarify the mechanism of NS3pro activation.Keywords
This publication has 13 references indexed in Scilit:
- Peptide inhibitors of dengue virus NS3 protease. Part 2: SAR study of tetrapeptide aldehyde inhibitorsBioorganic & Medicinal Chemistry Letters, 2005
- Enzymatic Characterization and Homology Model of a Catalytically Active Recombinant West Nile Virus NS3 ProteasePublished by Elsevier BV ,2004
- An NS3 protease inhibitor with antiviral effects in humans infected with hepatitis C virusNature, 2003
- Activity of Recombinant Dengue 2 Virus NS3 Protease in the Presence of a Truncated NS2B Co-factor, Small Peptide Substrates, and InhibitorsPublished by Elsevier BV ,2001
- RETRACTED: Crystal structure of dengue virus NS3 protease in complex with a bowman-birk inhibitor: implications for flaviviral polyprotein processing and drug designJournal of Molecular Biology, 2000
- Purified NS2B/NS3 Serine Protease of Dengue Virus Type 2 Exhibits Cofactor NS2B Dependence for Cleavage of Substrates with Dibasic Amino Acids in VitroPublished by Elsevier BV ,2000
- Dengue Virus NS3 Serine ProteasePublished by Elsevier BV ,1999
- Crystal Structure of the Hepatitis C Virus NS3 Protease Domain Complexed with a Synthetic NS4A Cofactor PeptideCell, 1996
- The Crystal Structure of Hepatitis C Virus NS3 Proteinase Reveals a Trypsin-like Fold and a Structural Zinc Binding SiteCell, 1996
- FLAVIVIRUS GENOME ORGANIZATION, EXPRESSION, AND REPLICATIONAnnual Review of Microbiology, 1990