Pre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes

RNA-dependent RNA polymerases from segmented negative stranded RNA viruses catalyze genome replication and viral transcription. Here, the authors present the cryo-EM structure of full-length La Crosse virus polymerase and structurally characterize the pre-initiation and elongation states, which is o...

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Autores principales: Benoît Arragain, Grégory Effantin, Piotr Gerlach, Juan Reguera, Guy Schoehn, Stephen Cusack, Hélène Malet
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/5cb62ccd989949bab8fe52127c04e712
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spelling oai:doaj.org-article:5cb62ccd989949bab8fe52127c04e7122021-12-02T15:33:16ZPre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes10.1038/s41467-020-17349-42041-1723https://doaj.org/article/5cb62ccd989949bab8fe52127c04e7122020-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-17349-4https://doaj.org/toc/2041-1723RNA-dependent RNA polymerases from segmented negative stranded RNA viruses catalyze genome replication and viral transcription. Here, the authors present the cryo-EM structure of full-length La Crosse virus polymerase and structurally characterize the pre-initiation and elongation states, which is of interest for the development of polymerase inhibitors.Benoît ArragainGrégory EffantinPiotr GerlachJuan RegueraGuy SchoehnStephen CusackHélène MaletNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Benoît Arragain
Grégory Effantin
Piotr Gerlach
Juan Reguera
Guy Schoehn
Stephen Cusack
Hélène Malet
Pre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes
description RNA-dependent RNA polymerases from segmented negative stranded RNA viruses catalyze genome replication and viral transcription. Here, the authors present the cryo-EM structure of full-length La Crosse virus polymerase and structurally characterize the pre-initiation and elongation states, which is of interest for the development of polymerase inhibitors.
format article
author Benoît Arragain
Grégory Effantin
Piotr Gerlach
Juan Reguera
Guy Schoehn
Stephen Cusack
Hélène Malet
author_facet Benoît Arragain
Grégory Effantin
Piotr Gerlach
Juan Reguera
Guy Schoehn
Stephen Cusack
Hélène Malet
author_sort Benoît Arragain
title Pre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes
title_short Pre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes
title_full Pre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes
title_fullStr Pre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes
title_full_unstemmed Pre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes
title_sort pre-initiation and elongation structures of full-length la crosse virus polymerase reveal functionally important conformational changes
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/5cb62ccd989949bab8fe52127c04e712
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