Dynamics: the missing link between structure and function of the viral RNA-dependent RNA polymerase?

Curr Opin Struct Biol. 2009 Dec;19(6):768-74. doi: 10.1016/j.sbi.2009.10.012. Epub 2009 Nov 10.

Abstract

The structural basis for nucleotide incorporation fidelity remains an open question for all nucleic acid polymerases. Addressing this question for the viral RNA-dependent RNA polymerase (RdRp) is of particular, practical significance because it is a determinant of sensitivity to antiviral nucleosides and may be a determinant of viral virulence. All polymerases are thought to employ the same catalytic mechanism, but the rate of nucleotide incorporation can vary substantially. Here we review some of the recent work with the RdRp that leads us to suggest that structure provides only a partial understanding of RdRp function and dynamics may be the missing link.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Antiviral Agents / pharmacology
  • Catalytic Domain
  • Humans
  • Nucleotides / metabolism
  • RNA-Dependent RNA Polymerase / chemistry*
  • RNA-Dependent RNA Polymerase / metabolism*
  • Structure-Activity Relationship
  • Viruses / drug effects
  • Viruses / enzymology*
  • Viruses / metabolism

Substances

  • Antiviral Agents
  • Nucleotides
  • RNA-Dependent RNA Polymerase