1887

Abstract

NS3 of hepatitis C virus (HCV) is a serine protease that carries out the proteolytic processing of the nonstructural proteins of the HCV polyprotein. Deletion analysis of the N terminus of NS2,3,4 fusion protein revealed that the N-terminal boundary of the active protease resides between amino acids 1050 and 1083. The processing patterns of internal deletion mutants of NS2,3,4 indicated that the C terminus of the enzymically active protease resides between amino acids 1115 and 1218. The N- and C-terminal boundaries of the protease were also confirmed by determining the -cleavage activity of internally deleted NS3,4. NS3 protease activity was inhibited by Cu but was slightly enhanced by Zn. This report provides a possible approach for development of antiviral agents based on protease inhibitors.

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/content/journal/jgv/10.1099/0022-1317-76-4-985
1995-04-01
2019-11-12
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http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-76-4-985
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