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. 1997 Aug;71(8):6264–6266. doi: 10.1128/jvi.71.8.6264-6266.1997

A point mutation abolishes the helicase but not the nucleoside triphosphatase activity of hepatitis C virus NS3 protein.

G M Heilek 1, M G Peterson 1
PMCID: PMC191896  PMID: 9223530

Abstract

The NS3 protein of hepatitis C virus contains a bipartite structure consisting of an N-terminal serine protease and a C-terminal DEAD box helicase. We show that the C-terminal domain has ATPase and panhelicase activities. The integrity of the helicase function is dependent on the conserved DEAD motif and can be abolished by a His-Ala point mutation, leaving a fully functional nucleoside triphosphatase.

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Selected References

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