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PubMed · 9864043

Hepatitis C virus NS3/4A protease.

A D Kwong·J L Kim·G Rao·D Lipovsek·S A Raybuck
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Abstract

Despite an urgent medical need, a broadly effective anti-viral therapy for the treatment of infections with hepatitis C viruses (HCVs) has yet to be developed. One of the approaches to anti-HCV drug discovery is the design and development of specific small molecule drugs to inhibit the proteolytic processing of the HCV polyprotein. This proteolytic processing is catalyzed by a chymotrypsin-like serine protease which is located in the N-terminal region of non-structural protein 3 (NS3). This protease domain forms a tight, non-covalent complex with NS4A, a 54 amino acid activator of NS3 protease. The C-terminal two-thirds of the NS3 protein contain a helicase and a nucleic acid-stimulated nucleoside triphosphatase (NTPase) activities which are probably involved in viral replication. This review will focus on the structure and function of the serine protease activity of NS3/4A and the development of inhibitors of this activity.

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Amino Acid SequenceAnimalsBinding SitesBiological AssayCatalytic DomainEnzyme InhibitorsHepacivirusHepatitis CHumansModels, MolecularMolecular Sequence DataProtein ConformationSerine EndopeptidasesSubstrate SpecificityViral Nonstructural ProteinsNucleoside-TriphosphataseDEAD-box RNA HelicasesViral ProteasesJournal ArticleReview

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A D Kwong, J L Kim, G Rao, D Lipovsek, S A Raybuck. 1998. Hepatitis C virus NS3/4A protease.. https://doi.org/10.1016/s0166-3542(98)00043-6

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