NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B.

Bessa, Luiza M

NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B. [electronic resource] - The Journal of biological chemistry 11 2017 - 18024-18043 p. digital

Publication Type: Journal Article

1083-351X

10.1074/jbc.M117.813766 doi


Allosteric Regulation--drug effects
Allosteric Site--drug effects
Antiviral Agents--chemistry
Enzyme Inhibitors--chemistry
Gene Deletion
Hepacivirus--enzymology
Intrinsically Disordered Proteins--chemistry
Isoleucine--chemistry
Models, Molecular
Mutagenesis, Site-Directed
Nuclear Magnetic Resonance, Biomolecular
Oligoribonucleotides--chemistry
Peptide Fragments--antagonists & inhibitors
Point Mutation
Protein Conformation
Protein Interaction Domains and Motifs
Protein Refolding--drug effects
Pyrones--chemistry
RNA-Dependent RNA Polymerase--antagonists & inhibitors
Recombinant Proteins--chemistry
Solubility
Triazoles--chemistry
Viral Nonstructural Proteins--antagonists & inhibitors