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Structural basis of Zika virus methyltransferase inhibition by sinefungin
K. Hercik, J. Brynda, R. Nencka, E. Boura,
Jazyk angličtina Země Rakousko
Typ dokumentu časopisecké články
NLK
ProQuest Central
od 2002-01-01 do Před 1 rokem
Medline Complete (EBSCOhost)
od 2000-01-01 do Před 1 rokem
Health & Medicine (ProQuest)
od 2002-01-01 do Před 1 rokem
Public Health Database (ProQuest)
od 2002-01-01 do Před 1 rokem
- MeSH
- adenosin analogy a deriváty chemie MeSH
- inhibitory enzymů chemie MeSH
- methyltransferasy antagonisté a inhibitory MeSH
- molekulární modely MeSH
- vazba proteinů MeSH
- vazebná místa MeSH
- virus zika enzymologie MeSH
- Publikační typ
- časopisecké články MeSH
Zika virus is considered a major global threat to human kind. Here, we present a crystal structure of one of its essential enzymes, the methyltransferase, with the inhibitor sinefungin. This structure, together with previously solved structures with bound substrates, will provide the information needed for rational inhibitor design. Based on the structural data we suggest the modification of the adenine moiety of sinefungin to increase selectivity and to covalently link it to a GTP analogue, to increase the affinity of the synthesized compounds.
Citace poskytuje Crossref.org
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