The rearrangement of motif F in the flavivirus RNA-directed RNA polymerase.

Int J Biol Macromol

Limnological Institute, Siberian Branch of Russian Academy of Sciences, 664033 Irkutsk, Russia.

Published: March 2018

AI Article Synopsis

  • The NS5 protein in flaviviruses is crucial for RNA replication and is a key target for drug development.
  • Understanding how the two domains of NS5—the RNA-dependent RNA polymerase and the methyltransferase—interact is essential for revealing NS5's functions in the viral life cycle.
  • Studies indicate that a conserved motif in NS5 may function as a "lock" that regulates domain rearrangement and acts as a switch for the protein's enzymatic activities.

Article Abstract

In the flavivirus genus, the non-structural protein NS5 plays a central role in RNA viral replication and constitutes a major target for drug discovery. One of the prime challenges in the study of NS5 protein is to investigate the interplay between the two protein domains, namely, the RNA-dependent RNA polymerase (RdRp) domain and the methyltransferase (MTase) domain. These investigations could clarify the multiple roles of NS5 protein in the virus life cycle. Here we present the results of sequence analyses and structural bioinformatics studies of NS5 protein, which suggest that the conserved motif F in the NS5 protein could act as a lock which controls the rearrangement of the domains and as a switch in the protein enzymatic activity.

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http://dx.doi.org/10.1016/j.ijbiomac.2017.11.009DOI Listing

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