Abstract
We present here our current understanding of the NS5A-D2 domain of the hepatitis C virus. Whereas this protein domain is globally unstructured as assessed by macroscopic techniques such as size exclusion chromatography, circular dichroism and homonuclear NMR spectroscopy, high resolution triple resonance spectroscopy allows the identification of a small region of residual structure. This region corresponds moreover to the most conserved sequence over the different genotypes of the virus, underscoring its functional importance. We show that it forms an anchoring point for the host cell cyclophilin prolyl cis/trans isomerase, providing a molecular basis for the use of cyclophilin inhibitors in an antiviral strategy.
Keywords: Hepatitis C Virus, NS5A, Domain 2, unstructured, NMR, Circular dichroism
Protein & Peptide Letters
Title: The Domain 2 of the HCV NS5A Protein Is Intrinsically Unstructured
Volume: 17 Issue: 8
Author(s): Xavier Hanoulle, Aurelie Badillo, Dries Verdegem, Francois Penin and Guy Lippens
Affiliation:
Keywords: Hepatitis C Virus, NS5A, Domain 2, unstructured, NMR, Circular dichroism
Abstract: We present here our current understanding of the NS5A-D2 domain of the hepatitis C virus. Whereas this protein domain is globally unstructured as assessed by macroscopic techniques such as size exclusion chromatography, circular dichroism and homonuclear NMR spectroscopy, high resolution triple resonance spectroscopy allows the identification of a small region of residual structure. This region corresponds moreover to the most conserved sequence over the different genotypes of the virus, underscoring its functional importance. We show that it forms an anchoring point for the host cell cyclophilin prolyl cis/trans isomerase, providing a molecular basis for the use of cyclophilin inhibitors in an antiviral strategy.
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Cite this article as:
Hanoulle Xavier, Badillo Aurelie, Verdegem Dries, Penin Francois and Lippens Guy, The Domain 2 of the HCV NS5A Protein Is Intrinsically Unstructured, Protein & Peptide Letters 2010; 17 (8) . https://dx.doi.org/10.2174/092986610791498920
DOI https://dx.doi.org/10.2174/092986610791498920 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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