Cargando…
Structure of NS3 helicase from Zika virus
The Zika virus has emerged as a pathogen of major health concern. We present a high-resolution (1.62Å) crystal structure of the RNA helicase from the French Polynesia strain. The structure is similar to that of the RNA helicase from Dengue virus, with variability in the conformations of loops typica...
Autores principales: | , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5085289/ https://www.ncbi.nlm.nih.gov/pubmed/27399257 http://dx.doi.org/10.1038/nsmb.3258 |
_version_ | 1782463544690737152 |
---|---|
author | Jain, Rinku Coloma, Javier García-Sastre, Adolfo Aggarwal, Aneel K. |
author_facet | Jain, Rinku Coloma, Javier García-Sastre, Adolfo Aggarwal, Aneel K. |
author_sort | Jain, Rinku |
collection | PubMed |
description | The Zika virus has emerged as a pathogen of major health concern. We present a high-resolution (1.62Å) crystal structure of the RNA helicase from the French Polynesia strain. The structure is similar to that of the RNA helicase from Dengue virus, with variability in the conformations of loops typically involved in ATP and RNA binding. We identify druggable “hotspots” that are well-suited for in-silico and/or fragment-based high throughput drug discovery. |
format | Online Article Text |
id | pubmed-5085289 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
record_format | MEDLINE/PubMed |
spelling | pubmed-50852892017-01-11 Structure of NS3 helicase from Zika virus Jain, Rinku Coloma, Javier García-Sastre, Adolfo Aggarwal, Aneel K. Nat Struct Mol Biol Article The Zika virus has emerged as a pathogen of major health concern. We present a high-resolution (1.62Å) crystal structure of the RNA helicase from the French Polynesia strain. The structure is similar to that of the RNA helicase from Dengue virus, with variability in the conformations of loops typically involved in ATP and RNA binding. We identify druggable “hotspots” that are well-suited for in-silico and/or fragment-based high throughput drug discovery. 2016-07-11 2016-08 /pmc/articles/PMC5085289/ /pubmed/27399257 http://dx.doi.org/10.1038/nsmb.3258 Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Jain, Rinku Coloma, Javier García-Sastre, Adolfo Aggarwal, Aneel K. Structure of NS3 helicase from Zika virus |
title | Structure of NS3 helicase from Zika virus |
title_full | Structure of NS3 helicase from Zika virus |
title_fullStr | Structure of NS3 helicase from Zika virus |
title_full_unstemmed | Structure of NS3 helicase from Zika virus |
title_short | Structure of NS3 helicase from Zika virus |
title_sort | structure of ns3 helicase from zika virus |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5085289/ https://www.ncbi.nlm.nih.gov/pubmed/27399257 http://dx.doi.org/10.1038/nsmb.3258 |
work_keys_str_mv | AT jainrinku structureofns3helicasefromzikavirus AT colomajavier structureofns3helicasefromzikavirus AT garciasastreadolfo structureofns3helicasefromzikavirus AT aggarwalaneelk structureofns3helicasefromzikavirus |