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Int. J. Mol. Sci. 2013, 14(7), 13282-13306; doi:10.3390/ijms140713282
Review

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

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Received: 22 April 2013; in revised form: 4 June 2013 / Accepted: 13 June 2013 / Published: 26 June 2013
(This article belongs to the Special Issue Protein Folding 2015)
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Abstract: 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.
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
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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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.

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.

Chicago/Turabian Style

Vega, Sonia; Neira, Jose L.; Marcuello, Carlos; Lostao, Anabel; Abian, Olga; Velazquez-Campoy, Adrian. 2013. "NS3 Protease from Hepatitis C Virus: Biophysical Studies on an Intrinsically Disordered Protein Domain." Int. J. Mol. Sci. 14, no. 7: 13282-13306.


Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert