Review
doi: 10.1007/978-3-642-59605-6_9.
Structure and function of hepatitis C virus NS3 helicase
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- PMID: 10592661
- DOI: 10.1007/978-3-642-59605-6_9
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Review
Structure and function of hepatitis C virus NS3 helicase
Curr Top Microbiol Immunol.
2000.
Abstract
Hepatitis C Virus helicase activity has been mapped to the COOH-terminal 450 residues of the NS3 protein. Due to its complexity and presumed essentiality for viral replication, the helicase is an attractive target for drug discovery. The elucidation of the atomic structure of the HCV NS3 helicase in complex with oligonucleotide and with ADP has helped clarify our understanding of potential sites for inhibitor binding. Molecular details of the mechanism of this enzyme, and in particular, a better understanding of the mechanism by which ATP hydrolysis is coupled to unwinding of double-stranded substrate may facilitate more efficient structure-based drug design.
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