Mechanism of SARS-CoV-2 polymerase stalling by remdesivir

Remdesivir is a nucleoside analog that inhibits the SARS-CoV-2 RNA dependent RNA polymerase (RdRp) and is used as a drug to treat COVID19 patients. Here, the authors provide insights into the mechanism of remdesivir-induced RdRp stalling by determining the cryo-EM structures of SARS-CoV-2 RdRp with...

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Autores principales: Goran Kokic, Hauke S. Hillen, Dimitry Tegunov, Christian Dienemann, Florian Seitz, Jana Schmitzova, Lucas Farnung, Aaron Siewert, Claudia Höbartner, Patrick Cramer
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Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/8b3f1fceaaca4cfa95f1314132c6731b
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spelling oai:doaj.org-article:8b3f1fceaaca4cfa95f1314132c6731b2021-12-02T15:22:39ZMechanism of SARS-CoV-2 polymerase stalling by remdesivir10.1038/s41467-020-20542-02041-1723https://doaj.org/article/8b3f1fceaaca4cfa95f1314132c6731b2021-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20542-0https://doaj.org/toc/2041-1723Remdesivir is a nucleoside analog that inhibits the SARS-CoV-2 RNA dependent RNA polymerase (RdRp) and is used as a drug to treat COVID19 patients. Here, the authors provide insights into the mechanism of remdesivir-induced RdRp stalling by determining the cryo-EM structures of SARS-CoV-2 RdRp with bound RNA molecules that contain remdesivir at defined positions and observe that addition of the fourth nucleotide following remdesivir incorporation into the RNA product is impaired by a barrier to further RNA translocation.Goran KokicHauke S. HillenDimitry TegunovChristian DienemannFlorian SeitzJana SchmitzovaLucas FarnungAaron SiewertClaudia HöbartnerPatrick CramerNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-7 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Goran Kokic
Hauke S. Hillen
Dimitry Tegunov
Christian Dienemann
Florian Seitz
Jana Schmitzova
Lucas Farnung
Aaron Siewert
Claudia Höbartner
Patrick Cramer
Mechanism of SARS-CoV-2 polymerase stalling by remdesivir
description Remdesivir is a nucleoside analog that inhibits the SARS-CoV-2 RNA dependent RNA polymerase (RdRp) and is used as a drug to treat COVID19 patients. Here, the authors provide insights into the mechanism of remdesivir-induced RdRp stalling by determining the cryo-EM structures of SARS-CoV-2 RdRp with bound RNA molecules that contain remdesivir at defined positions and observe that addition of the fourth nucleotide following remdesivir incorporation into the RNA product is impaired by a barrier to further RNA translocation.
format article
author Goran Kokic
Hauke S. Hillen
Dimitry Tegunov
Christian Dienemann
Florian Seitz
Jana Schmitzova
Lucas Farnung
Aaron Siewert
Claudia Höbartner
Patrick Cramer
author_facet Goran Kokic
Hauke S. Hillen
Dimitry Tegunov
Christian Dienemann
Florian Seitz
Jana Schmitzova
Lucas Farnung
Aaron Siewert
Claudia Höbartner
Patrick Cramer
author_sort Goran Kokic
title Mechanism of SARS-CoV-2 polymerase stalling by remdesivir
title_short Mechanism of SARS-CoV-2 polymerase stalling by remdesivir
title_full Mechanism of SARS-CoV-2 polymerase stalling by remdesivir
title_fullStr Mechanism of SARS-CoV-2 polymerase stalling by remdesivir
title_full_unstemmed Mechanism of SARS-CoV-2 polymerase stalling by remdesivir
title_sort mechanism of sars-cov-2 polymerase stalling by remdesivir
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/8b3f1fceaaca4cfa95f1314132c6731b
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