HCV NS3/4A protease genotype 1b, recombinant
- Cat.Number : AS-61017-5
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NS3 protease of hepatitis C virus (HCV), located on the N-terminal domain of HCV NS3, is responsible for the cleavage at the NS3/NS4A, NS4A/NS4B, NS4B/NS5A, and NS5A/NS5B sites of the nonstructural protein. The HCV NS3 is a chymotrypsin-like serine protease. It requires a cofactor, a 54 amino acid NS4 protein, to reach its optimal activity. The X-ray crystal structure studies show that NS3 forms a tight non-covalent complex with NS4. The NS3/4A protease is essential for viral replication and the formation of infectious viral particles, and thus has been considered as one of the most attractive targets for anti-HCV therapy.
The recombinant HCV NS3/4A protease (genotype 1b, strain: HC-J4; NCBI Accession: AF054247) was expressed in E. Coli. HCV NS3/4A protease is a 217 amino acid fusion protein (22.7 kDa) with NS4A co-factor fused to the N-terminus of NS3 protease domain. Therefore, HCV NS3/4A protease is in active form and the pre-activation by pep4A or pep4AK is not necessary. 5-20 ng of HCV NS3/4A protease is sufficient for FRET-based activity assays (SensoLyte® HCV protease assay).
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Citations
HCV Protease Inhibitory, Cytotoxic and Apoptosis-Inducing Effects of Oleanolic Acid Derivatives
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Phytother Res. . 2009 Apr 01 ; 23(4) 582 | DOI : 10.1002/ptr.2657
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Development of a cell-based hepatitis C virus infection fluorescent resonance energy transfer assay for high-throughput antiviral compound screening.
Antimicrob Agents Chemother. . 2009 Jul 20 ; 53(10) 4311 | DOI : 10.1128/AAC.00495-09
- X. Yu
Triterpenes from Cynomorium songaricium--analysis of HCV protease inhibitory activity, quantification, and content change under the influence of heating.
J Nat Med . 2008 Jul 04 ; 63(1) 9 | DOI : 10.1007/s11418-008-0267-7
- C. Ma
Hepatitis C Virus NS2 Protein Contributes to Virus Particle Assembly via Opposing Epistatic Interactions with the E1-E2 Glycoprotein and NS3-NS4A Enzyme Complexes
J Virol. . 2009 Jun 10 ; 83(17) 8379 | DOI : 10.1128/JVI.00891-09
- T. Phan
References
Crystal Structure of the Hepatitis C Virus NS3 Protease Domain Complexed with a Synthetic NS4A Cofactor Peptide
Cell . 1996 Oct 18 ; 87(2) 343 | DOI : https://doi.org/10.1016/S0092-8674(00)81351-3
- JL. Kim
- et al
Mechanistic Role of an NS4A Peptide Cofactor with the Truncated NS3 Protease of Hepatitis C Virus: Elucidation of the NS4A Stimulatory Effect via Kinetic Analysis and Inhibitor Mapping
Biochemistry . 1997 Aug 05 ; 36(31) 9340 | DOI : https://doi.org/10.1021/bi963054n
- JA. Landro
- et al
The Hepatitis C Virus Encodes a Serine Protease Involved in Processing of the Putative Nonstructural Proteins from the Viral Polyprotein Precursor
Biochem.Biophys.Res.Commun. . 1993 Apr 30 ; 192(2) 399 | DOI : https://doi.org/10.1006/bbrc.1993.1429
- MR. Eckart
- et al
The Crystal Structure of Hepatitis C Virus NS3 Proteinase Reveals a Trypsin-like Fold and a Structural Zinc Binding Site
Cell . 1996 Oct 18 ; 87(2) 331 | DOI : https://doi.org/10.1016/S0092-8674(00)81350-1
- RA. Love
- et al
Nonstructural protein 3 of the hepatitis C virus encodes a serine-type proteinase required for cleavage at the NS3/4 and NS4/5 junctions
J Virol . 1993 Jul 01 ; 67(7) 3835 | DOI : 10.1128/JVI.67.7.3835-3844.1993
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- et al