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Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus.
Erbel, Paul; Schiering, Nikolaus; D'Arcy, Allan; Renatus, Martin; Kroemer, Markus; Lim, Siew Pheng; Yin, Zheng; Keller, Thomas H; Vasudevan, Subhash G; Hommel, Ulrich.
Afiliación
  • Erbel P; Novartis Institutes for Biomedical Research, Protease Platform, 4002 Basel, Switzerland.
Nat Struct Mol Biol ; 13(4): 372-3, 2006 Apr.
Article en En | MEDLINE | ID: mdl-16532006
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.
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Bases de datos: MEDLINE Asunto principal: Virus del Nilo Occidental / Serina Endopeptidasas / Proteínas no Estructurales Virales / Virus del Dengue Idioma: En Revista: Nat Struct Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2006 Tipo del documento: Article País de afiliación: Suiza
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Bases de datos: MEDLINE Asunto principal: Virus del Nilo Occidental / Serina Endopeptidasas / Proteínas no Estructurales Virales / Virus del Dengue Idioma: En Revista: Nat Struct Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2006 Tipo del documento: Article País de afiliación: Suiza