IDENTIFICATION OF THE PROTEASE DOMAIN IN NS3 OF HEPATITIS-C VIRUS
SCIE
SCOPUS
- Title
- IDENTIFICATION OF THE PROTEASE DOMAIN IN NS3 OF HEPATITIS-C VIRUS
- Authors
- HAN, DS; HAHM, B; RHO, HM; JANG, SK
- Date Issued
- 1995-04
- Publisher
- SOC GENERAL MICROBIOLOGY
- 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 tr ans-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.
- Keywords
- NON-B-HEPATITIS; NON-A; HEPATOCELLULAR-CARCINOMA; STRUCTURAL REGION; MAMMALIAN-CELLS; CORE PROTEIN; ENTRY SITE; EXPRESSION; POLYPROTEIN; RNA
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/21815
- DOI
- 10.1099/0022-1317-76-4-985
- ISSN
- 0022-1317
- Article Type
- Article
- Citation
- JOURNAL OF GENERAL VIROLOGY, vol. 76, no. 4, page. 985 - 993, 1995-04
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- There are no files associated with this item.
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