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NS3 Protease from Hepatitis C Virus: Biophysical Studies on an Intrinsically Disordered Protein Domain

1
Institute of Biocomputation and Physics of Complex Systems (BIFI), Joint Unit BIFI-IQFR (CSIC), University of Zaragoza, Zaragoza 50018, Spain
2
Institute of Molecular and Cell Biology, Miguel Hernandez University, Elche (Alicante) 03202, Spain
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Advanced Microscopy Laboratory (LMA), Institute of Nanoscience of Aragon (INA), University of Zaragoza, Zaragoza 50018, Spain
4
ARAID Foundation, Government of Aragon, Zaragoza 50018, Spain
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IIS Aragon–Aragon Health Science Institute (I+CS), Zaragoza 50009, Spain
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Network Biomedical Research Center on Hepatic and Digestive Diseases (CIBERehd), Barcelona 08036, Spain
7
Department of Biochemistry and Cellular and Molecular Biology, Faculty of Sciences, University of Zaragoza, Zaragoza 50009, Spain
*
Authors to whom correspondence should be addressed.
Int. J. Mol. Sci. 2013, 14(7), 13282-13306; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms140713282
Received: 22 April 2013 / Revised: 4 June 2013 / Accepted: 13 June 2013 / Published: 26 June 2013
(This article belongs to the Collection Protein Folding)
The nonstructural protein 3 (NS3) from the hepatitis C virus (HCV) is responsible for processing the non-structural region of the viral precursor polyprotein in infected hepatic cells. NS3 protease activity, located at the N-terminal domain, is a zinc-dependent serine protease. A zinc ion, required for the hydrolytic activity, has been considered as a structural metal ion essential for the structural integrity of the protein. In addition, NS3 interacts with another cofactor, NS4A, an accessory viral protein that induces a conformational change enhancing the hydrolytic activity. Biophysical studies on the isolated protease domain, whose behavior is similar to that of the full-length protein (e.g., catalytic activity, allosteric mechanism and susceptibility to inhibitors), suggest that a considerable global conformational change in the protein is coupled to zinc binding. Zinc binding to NS3 protease can be considered as a folding event, an extreme case of induced-fit binding. Therefore, NS3 protease is an intrinsically (partially) disordered protein with a complex conformational landscape due to its inherent plasticity and to the interaction with its different effectors. Here we summarize the results from a detailed biophysical characterization of this enzyme and present new experimental data. View Full-Text
Keywords: NS3 protease; protein folding and stability; ligand binding; conformational landscape; intrinsically disordered protein NS3 protease; protein folding and stability; ligand binding; conformational landscape; intrinsically disordered protein
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MDPI and ACS Style

Vega, S.; Neira, J.L.; Marcuello, C.; Lostao, A.; Abian, O.; Velazquez-Campoy, A. NS3 Protease from Hepatitis C Virus: Biophysical Studies on an Intrinsically Disordered Protein Domain. Int. J. Mol. Sci. 2013, 14, 13282-13306. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms140713282

AMA Style

Vega S, Neira JL, Marcuello C, Lostao A, Abian O, Velazquez-Campoy A. NS3 Protease from Hepatitis C Virus: Biophysical Studies on an Intrinsically Disordered Protein Domain. International Journal of Molecular Sciences. 2013; 14(7):13282-13306. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms140713282

Chicago/Turabian Style

Vega, Sonia, Jose L. Neira, Carlos Marcuello, Anabel Lostao, Olga Abian, and Adrian Velazquez-Campoy. 2013. "NS3 Protease from Hepatitis C Virus: Biophysical Studies on an Intrinsically Disordered Protein Domain" International Journal of Molecular Sciences 14, no. 7: 13282-13306. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms140713282

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