Ontology highlight
ABSTRACT:
SUBMITTER: Frick DN
PROVIDER: S-EPMC3571657 | biostudies-literature | 2007 Jan
REPOSITORIES: biostudies-literature
Current issues in molecular biology 20070101 1
The C-terminal portion of hepatitis C virus (HCV) nonstructural protein 3 (NS3) forms a three domain polypeptide that possesses the ability to travel along RNA or single-stranded DNA (ssDNA) in a 3' to 5' direction. Fueled byATP hydrolysis, this movement allows the protein to displace complementary strands of DNA or RNA and proteins bound to the nucleic acid. HCV helicase shares two domains common to other motor proteins, one of which appears to rotate upon ATP binding. Several models have been ...[more]