| pubmed-article:16051821 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16051821 | lifeskim:mentions | umls-concept:C0011315 | lld:lifeskim |
| pubmed-article:16051821 | lifeskim:mentions | umls-concept:C0069156 | lld:lifeskim |
| pubmed-article:16051821 | lifeskim:mentions | umls-concept:C0920283 | lld:lifeskim |
| pubmed-article:16051821 | lifeskim:mentions | umls-concept:C0600499 | lld:lifeskim |
| pubmed-article:16051821 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:16051821 | lifeskim:mentions | umls-concept:C2699488 | lld:lifeskim |
| pubmed-article:16051821 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:16051821 | pubmed:dateCreated | 2005-7-29 | lld:pubmed |
| pubmed-article:16051821 | pubmed:abstractText | Dengue fever is an important emerging public health concern, with several million viral infections occurring annually, for which no effective therapy currently exists. The NS3 protein from Dengue virus is a multifunctional protein of 69 kDa, endowed with protease, helicase, and nucleoside 5'-triphosphatase (NTPase) activities. Thus, NS3 plays an important role in viral replication and represents a very interesting target for the development of specific antiviral inhibitors. We present the structure of an enzymatically active fragment of the Dengue virus NTPase/helicase catalytic domain to 2.4 A resolution. The structure is composed of three domains, displays an asymmetric distribution of charges on its surface, and contains a tunnel large enough to accommodate single-stranded RNA. Its C-terminal domain adopts a new fold compared to the NS3 helicase of hepatitis C virus, which has interesting implications for the evolution of the Flaviviridae replication complex. A bound sulfate ion reveals residues involved in the metal-dependent NTPase catalytic mechanism. Comparison with the NS3 hepatitis C virus helicase complexed to single-stranded DNA would place the 3' single-stranded tail of a nucleic acid duplex in the tunnel that runs across the basic face of the protein. A possible model for the unwinding mechanism is proposed. | lld:pubmed |
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| pubmed-article:16051821 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:16051821 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16051821 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16051821 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:16051821 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:16051821 | pubmed:author | pubmed-author:LescarJulienJ | lld:pubmed |
| pubmed-article:16051821 | pubmed:author | pubmed-author:VasudevanSubh... | lld:pubmed |
| pubmed-article:16051821 | pubmed:author | pubmed-author:WenDayingD | lld:pubmed |
| pubmed-article:16051821 | pubmed:author | pubmed-author:NanaoMaxM | lld:pubmed |
| pubmed-article:16051821 | pubmed:author | pubmed-author:SampathArunaA | lld:pubmed |
| pubmed-article:16051821 | pubmed:author | pubmed-author:XuTingT | lld:pubmed |
| pubmed-article:16051821 | pubmed:author | pubmed-author:ChenePatrickP | lld:pubmed |
| pubmed-article:16051821 | pubmed:author | pubmed-author:ChaoAlexA | lld:pubmed |
| pubmed-article:16051821 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16051821 | pubmed:volume | 79 | lld:pubmed |
| pubmed-article:16051821 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16051821 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16051821 | pubmed:pagination | 10278-88 | lld:pubmed |
| pubmed-article:16051821 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:16051821 | pubmed:meshHeading | pubmed-meshheading:16051821... | lld:pubmed |
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| pubmed-article:16051821 | pubmed:meshHeading | pubmed-meshheading:16051821... | lld:pubmed |
| pubmed-article:16051821 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16051821 | pubmed:articleTitle | Structure of the Dengue virus helicase/nucleoside triphosphatase catalytic domain at a resolution of 2.4 A. | lld:pubmed |
| pubmed-article:16051821 | pubmed:affiliation | School of Biological Sciences, Nanyang Technological University, 60, Nanyang Drive, Singapore 637551. | lld:pubmed |
| pubmed-article:16051821 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16051821 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:1494449 | entrezgene:pubmed | pubmed-article:16051821 | lld:entrezgene |
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