%0 Journal Article %A Han, Dae Sung %A Hahm, Bumsuk %A Rho, Hyune-Mo %A Jang, Sung Key %T Identification of the protease domain in NS3 of hepatitis C virus %D 1995 %J Journal of General Virology, %V 76 %N 4 %P 985-993 %@ 1465-2099 %R https://doi.org/10.1099/0022-1317-76-4-985 %I Microbiology Society, %X 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 trans-cleavage activity of internally deleted NS3,4. NS3 protease activity was inhibited by Cu2+ but was slightly enhanced by Zn2+. This report provides a possible approach for development of antiviral agents based on protease inhibitors. %U https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-76-4-985