Structures of NS5 Methyltransferase from Zika Virus

The Zika virus (ZIKV) poses a major public health emergency. To aid in the development of antivirals, we present two high-resolution crystal structures of the ZIKV NS5 methyltransferase: one bound to S-adenosylmethionine (SAM) and the other bound to SAM and 7-methyl guanosine diphosphate (7-MeGpp)....

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Detalles Bibliográficos
Autores principales: Coloma, Javier, Jain, Rinku, Rajashankar, Kanagalaghatta R., García-Sastre, Adolfo, Aggarwal, Aneel K.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2016
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5074680/
https://www.ncbi.nlm.nih.gov/pubmed/27633330
http://dx.doi.org/10.1016/j.celrep.2016.08.091
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author Coloma, Javier
Jain, Rinku
Rajashankar, Kanagalaghatta R.
García-Sastre, Adolfo
Aggarwal, Aneel K.
author_facet Coloma, Javier
Jain, Rinku
Rajashankar, Kanagalaghatta R.
García-Sastre, Adolfo
Aggarwal, Aneel K.
author_sort Coloma, Javier
collection PubMed
description The Zika virus (ZIKV) poses a major public health emergency. To aid in the development of antivirals, we present two high-resolution crystal structures of the ZIKV NS5 methyltransferase: one bound to S-adenosylmethionine (SAM) and the other bound to SAM and 7-methyl guanosine diphosphate (7-MeGpp). We identify features of ZIKV NS5 methyltransferase that lend to structure-based antiviral drug discovery. Specifically, SAM analogs with functionalities on the Cβ atom of the methionine portion of the molecules that occupy the RNA binding tunnel may provide better specificity relative to human RNA methyltransferases.
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spelling pubmed-50746802016-10-21 Structures of NS5 Methyltransferase from Zika Virus Coloma, Javier Jain, Rinku Rajashankar, Kanagalaghatta R. García-Sastre, Adolfo Aggarwal, Aneel K. Cell Rep Article The Zika virus (ZIKV) poses a major public health emergency. To aid in the development of antivirals, we present two high-resolution crystal structures of the ZIKV NS5 methyltransferase: one bound to S-adenosylmethionine (SAM) and the other bound to SAM and 7-methyl guanosine diphosphate (7-MeGpp). We identify features of ZIKV NS5 methyltransferase that lend to structure-based antiviral drug discovery. Specifically, SAM analogs with functionalities on the Cβ atom of the methionine portion of the molecules that occupy the RNA binding tunnel may provide better specificity relative to human RNA methyltransferases. 2016-09-12 2016-09-20 /pmc/articles/PMC5074680/ /pubmed/27633330 http://dx.doi.org/10.1016/j.celrep.2016.08.091 Text en http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Coloma, Javier
Jain, Rinku
Rajashankar, Kanagalaghatta R.
García-Sastre, Adolfo
Aggarwal, Aneel K.
Structures of NS5 Methyltransferase from Zika Virus
title Structures of NS5 Methyltransferase from Zika Virus
title_full Structures of NS5 Methyltransferase from Zika Virus
title_fullStr Structures of NS5 Methyltransferase from Zika Virus
title_full_unstemmed Structures of NS5 Methyltransferase from Zika Virus
title_short Structures of NS5 Methyltransferase from Zika Virus
title_sort structures of ns5 methyltransferase from zika virus
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5074680/
https://www.ncbi.nlm.nih.gov/pubmed/27633330
http://dx.doi.org/10.1016/j.celrep.2016.08.091
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