Source:http://linkedlifedata.com/resource/pubmed/id/11249710
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2001-3-15
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pubmed:abstractText |
An 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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1472-4472
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
289-96
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pubmed:dateRevised |
2005-11-16
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pubmed:meshHeading | |
pubmed:year |
2000
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pubmed:articleTitle |
Recent advances in the analysis of HCV NS5B RNA-dependent RNA polymerase.
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pubmed:affiliation |
Department of Structural Chemistry, Schering-Plough Research Institute, 2015 Galloping Hill Road, Kenilworth, NJ 07033, USA. Charles.Lesburg@spcorp.com
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pubmed:publicationType |
Journal Article,
Review
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