Han D S, Hahm B, Rho H M, Jang S K
Department of Life Science, Pohang University of Science and Technology, Kyungbuk, Korea.
J Gen Virol. 1995 Apr;76 ( Pt 4):985-93. doi: 10.1099/0022-1317-76-4-985.
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.
丙型肝炎病毒（HCV）的NS3是一种丝氨酸蛋白酶，负责对HCV多聚蛋白的非结构蛋白进行蛋白水解加工。对NS2、3、4融合蛋白N端的缺失分析表明，活性蛋白酶的N端边界位于氨基酸1050和1083之间。NS2、3、4内部缺失突变体的加工模式表明，酶活性蛋白酶的C端边界位于氨基酸1115和1218之间。通过测定内部缺失的NS3、4的反式切割活性，也证实了蛋白酶的N端和C端边界。NS3蛋白酶活性受到Cu2+的抑制，但受到Zn2+的轻微增强。本报告为基于蛋白酶抑制剂的抗病毒药物开发提供了一种可能的方法。
