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Default The casein kinase 2-dependent phosphorylation of NS5A domain 3 from hepatitis C virus followed by time-resolved NMR.

The casein kinase 2-dependent phosphorylation of NS5A domain 3 from hepatitis C virus followed by time-resolved NMR.

Related Articles The casein kinase 2-dependent phosphorylation of NS5A domain 3 from hepatitis C virus followed by time-resolved NMR.

Chembiochem. 2015 Dec 18;

Authors: Secci E, Luchinat E, Banci L

Abstract
Hepatitis C virus (HCV) chronically affects millions of individuals worldwide. The HCV non-structural protein 5A (NS5A) plays a critical role in the viral assembly pathway. Domain 3 (D3) of NS5A is an unstructured polypeptide responsible for the interaction with the core particle assembly structure. Casein kinase 2 (CK2) phosphorylates NS5A-D3 at multiple sites, which have been largely predicted and only indirectly observed. In order to identify the CK2-dependent phosphorylation sites, we monitored in vitro the reaction between NS5A-D3 and CK2 by time-resolved NMR. We unambiguously identified four serine residues as substrates of CK2. The apparent rate constant was determined for each site from the reaction curves. Serine 408 was quickly phosphorylated, while three other serines reacted slower. These results provide a starting point to elucidate the role of phosphorylation in the mechanisms of viral assembly, and in the modulation of the viral activity, at the molecular level.


PMID: 26684216 [PubMed - as supplied by publisher]



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