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pubmed-article:11249710pubmed:abstractTextAn RNA-dependent RNA polymerase denoted nonstructural protein 5B (NS5B) is the central enzyme in replication of the hepatitis C virus genome. Recent advances in the biochemical and structural understanding of NS5B include solubilization and purification of the full-length enzyme and various truncated forms. In vitro conditions for NS5B-catalyzed primer elongation using both homo- and heteropolymeric RNA templates were discovered. The crystal structure of the NS5B apoenzyme revealed a globular shape unique among polymerases, and implicated new structural features important for binding the RNA template and cognate ribonucleotide substrates. The crystallographic results also provided a structure-based framework for biochemical analyses and drug-design efforts. Finally, inhibitors of HCV RNA-dependent RNA polymerase have been reported.lld:pubmed
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pubmed-article:11249710pubmed:authorpubmed-author:WeberP CPClld:pubmed
pubmed-article:11249710pubmed:authorpubmed-author:LesburgC ACAlld:pubmed
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pubmed-article:11249710pubmed:pagination289-96lld:pubmed
pubmed-article:11249710pubmed:dateRevised2005-11-16lld:pubmed
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pubmed-article:11249710pubmed:articleTitleRecent advances in the analysis of HCV NS5B RNA-dependent RNA polymerase.lld:pubmed
pubmed-article:11249710pubmed:affiliationDepartment of Structural Chemistry, Schering-Plough Research Institute, 2015 Galloping Hill Road, Kenilworth, NJ 07033, USA. Charles.Lesburg@spcorp.comlld:pubmed
pubmed-article:11249710pubmed:publicationTypeJournal Articlelld:pubmed
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