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Article

Structural and biological identification of residues on the surface of NS3 helicase required for optimal replication of the hepatitis C virus.

The Journal of biological chemistry - 10 Feb 2006

Mackintosh Samuel G, Lu Jeff Zhiqiang, Jordan John B, Harrison Melody K, Sikora Bartek, Sharma Suresh D, Cameron Craig E, Raney Kevin D, Sakon Joshua

Abstract excerpt

The hepatitis C virus (HCV) nonstructural protein 3 (NS3) is a multifunctional enzyme with serine protease and DEXH/D-box helicase domains. A crystal structure of the NS3 helicase domain (NS3h) was generated in the presence of a single-stranded oligonucleotide long enough to accommodate binding of two molecules of enzyme. Several amino acid residues at the interface of the two NS3h molecules were identified that...

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Identifiers

PMID: 16306038
DOI: 10.1074/jbc.M512100200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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