{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Beran RK"],"funding":["Howard Hughes Medical Institute","NIGMS NIH HHS"],"pagination":["29929-37"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2573085"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["283(44)"],"pubmed_abstract":["Non-structural protein 3 (NS3) is a multifunctional enzyme possessing serine protease, NTPase, and RNA unwinding activities that are required for hepatitis C viral (HCV) replication. HCV non-structural protein 4A (NS4A) binds to the N-terminal NS3 protease domain to stimulate NS3 serine protease activity. In addition, the NS3 protease domain enhances the RNA binding, ATPase, and RNA unwinding activities of the C-terminal NS3 helicase domain (NS3hel). To determine whether NS3hel enhances the NS3 serine protease activity, we purified truncated and full-length NS3-4A complexes and examined their serine protease activities under a variety of salt and pH conditions. Our results indicate that the helicase domain enhances serine protease activity, just as the protease domain enhances helicase act"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Hepatitis C viral NS3-4A protease activity is enhanced by the NS3 helicase."],"pmcid":["PMC2573085"],"funding_grant_id":["GM60620","F32 GM071120-01A1"],"pubmed_authors":["Pyle AM","Beran RK"],"additional_accession":[]},"is_claimable":false,"name":"Hepatitis C viral NS3-4A protease activity is enhanced by the NS3 helicase.","description":"Non-structural protein 3 (NS3) is a multifunctional enzyme possessing serine protease, NTPase, and RNA unwinding activities that are required for hepatitis C viral (HCV) replication. HCV non-structural protein 4A (NS4A) binds to the N-terminal NS3 protease domain to stimulate NS3 serine protease activity. In addition, the NS3 protease domain enhances the RNA binding, ATPase, and RNA unwinding activities of the C-terminal NS3 helicase domain (NS3hel). To determine whether NS3hel enhances the NS3 serine protease activity, we purified truncated and full-length NS3-4A complexes and examined their serine protease activities under a variety of salt and pH conditions. Our results indicate that the helicase domain enhances serine protease activity, just as the protease domain enhances helicase act","dates":{"release":"2008-01-01T00:00:00Z","publication":"2008 Oct","modification":"2025-04-05T15:58:45.412Z","creation":"2019-03-27T00:19:04Z"},"accession":"S-EPMC2573085","cross_references":{"pubmed":["18723512"],"doi":["10.1074/jbc.M804065200"]}}