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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2010-7-19
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pubmed:abstractText |
Homology modeling of NS3 helicase in Tick-borne encephalitis virus using known protein crystal structure was done. Its 3-D structure was evaluated and validated using PROCHECK comprising amino acid residues in favored region of Ramachandran plot. Helicase forms a large family of proteins which ubiquitously distributes in wide variety of organisms. It plays crucial role in transcription and replication of single-stranded viral RNA genomes. Consequently, NS3 represents an interesting target for the development of specific antiviral inhibitors. Several helicase inhibiting effective drugs and analogs were selected and the active amino acid residues were targeted. Levovirin, Ribamidine and Ribavirin were found more potent to inhibit TBEV on the basis of robust binding affinity between protein-drug interactions. This finding may help to understand the nature of helicase and development of specific anti-TBEV therapies.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antiviral Agents,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/NS3 protein, flavivirus,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/Ribavirin,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Triazoles,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Nonstructural Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/levovirin valinate hydrochloride,
http://linkedlifedata.com/resource/pubmed/chemical/ribavirin amidine
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1913-2751
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pubmed:author |
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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 |
168-72
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pubmed:meshHeading |
pubmed-meshheading:20640834-Amino Acid Sequence,
pubmed-meshheading:20640834-Antiviral Agents,
pubmed-meshheading:20640834-Chemistry, Pharmaceutical,
pubmed-meshheading:20640834-Computer Simulation,
pubmed-meshheading:20640834-DNA Helicases,
pubmed-meshheading:20640834-Drug Evaluation, Preclinical,
pubmed-meshheading:20640834-Encephalitis Viruses, Tick-Borne,
pubmed-meshheading:20640834-Genome, Viral,
pubmed-meshheading:20640834-Molecular Conformation,
pubmed-meshheading:20640834-Molecular Sequence Data,
pubmed-meshheading:20640834-Monosaccharides,
pubmed-meshheading:20640834-RNA, Viral,
pubmed-meshheading:20640834-RNA Helicases,
pubmed-meshheading:20640834-Ribavirin,
pubmed-meshheading:20640834-Serine Endopeptidases,
pubmed-meshheading:20640834-Software,
pubmed-meshheading:20640834-Triazoles,
pubmed-meshheading:20640834-Viral Nonstructural Proteins
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pubmed:year |
2009
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pubmed:articleTitle |
Structural modeling of the NS 3 helicase of Tick-borne encephalitis virus and their virtual screening of potent drugs using molecular docking.
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pubmed:affiliation |
SYNTH-BIO group, Epigenomics Project, Universite d'Evry Val d'Essonne-CNRS-Genopole (R), 91034, EVRY Cedex, France.
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pubmed:publicationType |
Journal Article
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