Structure, mechanism and crystallographic fragment screening of the SARS-CoV-2 NSP13 helicase

The SARS-CoV-2 NSP13 helicase is essential for viral replication and of interest as a drug target. Here, the authors present the crystal structures of NSP13 in the apo form and bound to either phosphate or the non-hydrolysable ATP analog AMP-PNP and discuss the helicase mechanism. They also perform...

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Autores principales:	Joseph A. Newman, Alice Douangamath, Setayesh Yadzani, Yuliana Yosaatmadja, Antony Aimon, José Brandão-Neto, Louise Dunnett, Tyler Gorrie-stone, Rachael Skyner, Daren Fearon, Matthieu Schapira, Frank von Delft, Opher Gileadi
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/b0b0d159fff646579ffb503d1f3b7821
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spelling	oai:doaj.org-article:b0b0d159fff646579ffb503d1f3b78212021-12-02T18:50:56ZStructure, mechanism and crystallographic fragment screening of the SARS-CoV-2 NSP13 helicase10.1038/s41467-021-25166-62041-1723https://doaj.org/article/b0b0d159fff646579ffb503d1f3b78212021-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25166-6https://doaj.org/toc/2041-1723The SARS-CoV-2 NSP13 helicase is essential for viral replication and of interest as a drug target. Here, the authors present the crystal structures of NSP13 in the apo form and bound to either phosphate or the non-hydrolysable ATP analog AMP-PNP and discuss the helicase mechanism. They also perform a crystallographic fragment screening and identify 65 bound fragments, which could help in the design of new antiviral agents.Joseph A. NewmanAlice DouangamathSetayesh YadzaniYuliana YosaatmadjaAntony AimonJosé Brandão-NetoLouise DunnettTyler Gorrie-stoneRachael SkynerDaren FearonMatthieu SchapiraFrank von DelftOpher GileadiNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Joseph A. Newman Alice Douangamath Setayesh Yadzani Yuliana Yosaatmadja Antony Aimon José Brandão-Neto Louise Dunnett Tyler Gorrie-stone Rachael Skyner Daren Fearon Matthieu Schapira Frank von Delft Opher Gileadi Structure, mechanism and crystallographic fragment screening of the SARS-CoV-2 NSP13 helicase
description	The SARS-CoV-2 NSP13 helicase is essential for viral replication and of interest as a drug target. Here, the authors present the crystal structures of NSP13 in the apo form and bound to either phosphate or the non-hydrolysable ATP analog AMP-PNP and discuss the helicase mechanism. They also perform a crystallographic fragment screening and identify 65 bound fragments, which could help in the design of new antiviral agents.
format	article
author	Joseph A. Newman Alice Douangamath Setayesh Yadzani Yuliana Yosaatmadja Antony Aimon José Brandão-Neto Louise Dunnett Tyler Gorrie-stone Rachael Skyner Daren Fearon Matthieu Schapira Frank von Delft Opher Gileadi
author_facet	Joseph A. Newman Alice Douangamath Setayesh Yadzani Yuliana Yosaatmadja Antony Aimon José Brandão-Neto Louise Dunnett Tyler Gorrie-stone Rachael Skyner Daren Fearon Matthieu Schapira Frank von Delft Opher Gileadi
author_sort	Joseph A. Newman
title	Structure, mechanism and crystallographic fragment screening of the SARS-CoV-2 NSP13 helicase
title_short	Structure, mechanism and crystallographic fragment screening of the SARS-CoV-2 NSP13 helicase
title_full	Structure, mechanism and crystallographic fragment screening of the SARS-CoV-2 NSP13 helicase
title_fullStr	Structure, mechanism and crystallographic fragment screening of the SARS-CoV-2 NSP13 helicase
title_full_unstemmed	Structure, mechanism and crystallographic fragment screening of the SARS-CoV-2 NSP13 helicase
title_sort	structure, mechanism and crystallographic fragment screening of the sars-cov-2 nsp13 helicase
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/b0b0d159fff646579ffb503d1f3b7821
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Structure, mechanism and crystallographic fragment screening of the SARS-CoV-2 NSP13 helicase

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