Structural basis of RNA cap modification by SARS-CoV-2

Specific non-structural proteins (nsp) of SARS coronaviruses are involved in methylation of virally encoded mRNAs to mimic cellular mRNAs for protection against host innate immune restriction. Here, the authors present a high resolution structure of SARS-CoV-2 nsp16/nsp10 ternary complex in the pres...

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Autores principales: Thiruselvam Viswanathan, Shailee Arya, Siu-Hong Chan, Shan Qi, Nan Dai, Anurag Misra, Jun-Gyu Park, Fatai Oladunni, Dmytro Kovalskyy, Robert A. Hromas, Luis Martinez-Sobrido, Yogesh K. Gupta
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Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/1a2c5dcfc62842e8b013e549e88fbd22
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spelling oai:doaj.org-article:1a2c5dcfc62842e8b013e549e88fbd222021-12-02T16:17:53ZStructural basis of RNA cap modification by SARS-CoV-210.1038/s41467-020-17496-82041-1723https://doaj.org/article/1a2c5dcfc62842e8b013e549e88fbd222020-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-17496-8https://doaj.org/toc/2041-1723Specific non-structural proteins (nsp) of SARS coronaviruses are involved in methylation of virally encoded mRNAs to mimic cellular mRNAs for protection against host innate immune restriction. Here, the authors present a high resolution structure of SARS-CoV-2 nsp16/nsp10 ternary complex in the presence of cognate RNA substrate analogue and methyl donor, S-adenosyl methionine, revealing unique ligand-binding sites that may represent alternative targets for antiviral development.Thiruselvam ViswanathanShailee AryaSiu-Hong ChanShan QiNan DaiAnurag MisraJun-Gyu ParkFatai OladunniDmytro KovalskyyRobert A. HromasLuis Martinez-SobridoYogesh K. GuptaNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-7 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Thiruselvam Viswanathan
Shailee Arya
Siu-Hong Chan
Shan Qi
Nan Dai
Anurag Misra
Jun-Gyu Park
Fatai Oladunni
Dmytro Kovalskyy
Robert A. Hromas
Luis Martinez-Sobrido
Yogesh K. Gupta
Structural basis of RNA cap modification by SARS-CoV-2
description Specific non-structural proteins (nsp) of SARS coronaviruses are involved in methylation of virally encoded mRNAs to mimic cellular mRNAs for protection against host innate immune restriction. Here, the authors present a high resolution structure of SARS-CoV-2 nsp16/nsp10 ternary complex in the presence of cognate RNA substrate analogue and methyl donor, S-adenosyl methionine, revealing unique ligand-binding sites that may represent alternative targets for antiviral development.
format article
author Thiruselvam Viswanathan
Shailee Arya
Siu-Hong Chan
Shan Qi
Nan Dai
Anurag Misra
Jun-Gyu Park
Fatai Oladunni
Dmytro Kovalskyy
Robert A. Hromas
Luis Martinez-Sobrido
Yogesh K. Gupta
author_facet Thiruselvam Viswanathan
Shailee Arya
Siu-Hong Chan
Shan Qi
Nan Dai
Anurag Misra
Jun-Gyu Park
Fatai Oladunni
Dmytro Kovalskyy
Robert A. Hromas
Luis Martinez-Sobrido
Yogesh K. Gupta
author_sort Thiruselvam Viswanathan
title Structural basis of RNA cap modification by SARS-CoV-2
title_short Structural basis of RNA cap modification by SARS-CoV-2
title_full Structural basis of RNA cap modification by SARS-CoV-2
title_fullStr Structural basis of RNA cap modification by SARS-CoV-2
title_full_unstemmed Structural basis of RNA cap modification by SARS-CoV-2
title_sort structural basis of rna cap modification by sars-cov-2
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/1a2c5dcfc62842e8b013e549e88fbd22
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