Tipiracil binds to uridine site and inhibits Nsp15 endoribonuclease NendoU from SARS-CoV-2

Youngchang Kim, Jacek Wower, and colleagues explore the sequence specificity, metal ion dependence and catalytic mechanism of the Nsp15 endoribonuclease NendoU from SARS-CoV-2. The authors also solve five new crystal structures of the enzyme in complex with 5’UMP, 3’UMP, 5’cGpU, uridine 2′,3′-vanada...

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Autores principales:	Youngchang Kim, Jacek Wower, Natalia Maltseva, Changsoo Chang, Robert Jedrzejczak, Mateusz Wilamowski, Soowon Kang, Vlad Nicolaescu, Glenn Randall, Karolina Michalska, Andrzej Joachimiak
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/c2e1555f80bc4eb28bc2085247f56486
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spelling	oai:doaj.org-article:c2e1555f80bc4eb28bc2085247f564862021-12-02T14:11:03ZTipiracil binds to uridine site and inhibits Nsp15 endoribonuclease NendoU from SARS-CoV-210.1038/s42003-021-01735-92399-3642https://doaj.org/article/c2e1555f80bc4eb28bc2085247f564862021-02-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-01735-9https://doaj.org/toc/2399-3642Youngchang Kim, Jacek Wower, and colleagues explore the sequence specificity, metal ion dependence and catalytic mechanism of the Nsp15 endoribonuclease NendoU from SARS-CoV-2. The authors also solve five new crystal structures of the enzyme in complex with 5’UMP, 3’UMP, 5’cGpU, uridine 2′,3′-vanadate (transition state analog) and Tipiracil (uracil mimic), and demonstrate that Tipiracil inhibits SARS-CoV-2 Nsp15 by interacting with the uridine binding pocket in the enzyme’s active site.Youngchang KimJacek WowerNatalia MaltsevaChangsoo ChangRobert JedrzejczakMateusz WilamowskiSoowon KangVlad NicolaescuGlenn RandallKarolina MichalskaAndrzej JoachimiakNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Youngchang Kim Jacek Wower Natalia Maltseva Changsoo Chang Robert Jedrzejczak Mateusz Wilamowski Soowon Kang Vlad Nicolaescu Glenn Randall Karolina Michalska Andrzej Joachimiak Tipiracil binds to uridine site and inhibits Nsp15 endoribonuclease NendoU from SARS-CoV-2
description	Youngchang Kim, Jacek Wower, and colleagues explore the sequence specificity, metal ion dependence and catalytic mechanism of the Nsp15 endoribonuclease NendoU from SARS-CoV-2. The authors also solve five new crystal structures of the enzyme in complex with 5’UMP, 3’UMP, 5’cGpU, uridine 2′,3′-vanadate (transition state analog) and Tipiracil (uracil mimic), and demonstrate that Tipiracil inhibits SARS-CoV-2 Nsp15 by interacting with the uridine binding pocket in the enzyme’s active site.
format	article
author	Youngchang Kim Jacek Wower Natalia Maltseva Changsoo Chang Robert Jedrzejczak Mateusz Wilamowski Soowon Kang Vlad Nicolaescu Glenn Randall Karolina Michalska Andrzej Joachimiak
author_facet	Youngchang Kim Jacek Wower Natalia Maltseva Changsoo Chang Robert Jedrzejczak Mateusz Wilamowski Soowon Kang Vlad Nicolaescu Glenn Randall Karolina Michalska Andrzej Joachimiak
author_sort	Youngchang Kim
title	Tipiracil binds to uridine site and inhibits Nsp15 endoribonuclease NendoU from SARS-CoV-2
title_short	Tipiracil binds to uridine site and inhibits Nsp15 endoribonuclease NendoU from SARS-CoV-2
title_full	Tipiracil binds to uridine site and inhibits Nsp15 endoribonuclease NendoU from SARS-CoV-2
title_fullStr	Tipiracil binds to uridine site and inhibits Nsp15 endoribonuclease NendoU from SARS-CoV-2
title_full_unstemmed	Tipiracil binds to uridine site and inhibits Nsp15 endoribonuclease NendoU from SARS-CoV-2
title_sort	tipiracil binds to uridine site and inhibits nsp15 endoribonuclease nendou from sars-cov-2
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/c2e1555f80bc4eb28bc2085247f56486
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Tipiracil binds to uridine site and inhibits Nsp15 endoribonuclease NendoU from SARS-CoV-2

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