| Literature DB >> 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.Entities:
Mesh:
Substances:
Year: 1997 PMID: 9223530 PMCID: PMC191896
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103