Ontology highlight
ABSTRACT:
SUBMITTER: Liu D
PROVIDER: S-EPMC2366984 | biostudies-literature | 2003 Dec
REPOSITORIES: biostudies-literature
Liu Dingjiang D Windsor William T WT Wyss Daniel F DF
Protein science : a publication of the Protein Society 20031201 12
The NS3 helicase of the hepatitis C virus (HCV) unwinds double-stranded (ds) nucleic acid (NA) in an NTP-dependent fashion. Mechanistic details of this process are, however, largely unknown for the HCV helicase. We have studied the binding of dsDNA to an engineered version of subdomain 2 of the HCV helicase (d(2Delta)NS3h) by NMR and circular dichroism. Binding of dsDNA to d(2Delta)NS3h induces a local unfolding of helix (alpha(3)), which includes residues of conserved helicase motif VI (Q(460)R ...[more]