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Nonstructural protein 7 and 8 complexes of SARS‐CoV‐2

The pandemic outbreak of coronavirus disease 2019 (COVID‐19) across the world has led to millions of infection cases and caused a global public health crisis. Current research suggests that SARS‐CoV‐2 is a highly contagious coronavirus that spreads rapidly through communities. To understand the mech...

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Detalles Bibliográficos
Autores principales: Zhang, Changhui, Li, Li, He, Jun, Chen, Cheng, Su, Dan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley & Sons, Inc. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7980517/
https://www.ncbi.nlm.nih.gov/pubmed/33594727
http://dx.doi.org/10.1002/pro.4046
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author Zhang, Changhui
Li, Li
He, Jun
Chen, Cheng
Su, Dan
author_facet Zhang, Changhui
Li, Li
He, Jun
Chen, Cheng
Su, Dan
author_sort Zhang, Changhui
collection PubMed
description The pandemic outbreak of coronavirus disease 2019 (COVID‐19) across the world has led to millions of infection cases and caused a global public health crisis. Current research suggests that SARS‐CoV‐2 is a highly contagious coronavirus that spreads rapidly through communities. To understand the mechanisms of viral replication, it is imperative to investigate coronavirus viral replicase, a huge protein complex comprising up to 16 viral nonstructural and associated host proteins, which is the most promising antiviral target for inhibiting viral genome replication and transcription. Recently, several components of the viral replicase complex in SARS‐CoV‐2 have been solved to provide a basis for the design of new antiviral therapeutics. Here, we report the crystal structure of the SARS‐CoV‐2 nsp7+8 tetramer, which comprises two copies of each protein representing nsp7's full‐length and the C‐terminus of nsp8 owing to N‐terminus proteolysis during the process of crystallization. We also identified a long helical extension and highly flexible N‐terminal domain of nsp8, which is preferred for interacting with single‐stranded nucleic acids.
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spelling pubmed-79805172021-04-01 Nonstructural protein 7 and 8 complexes of SARS‐CoV‐2 Zhang, Changhui Li, Li He, Jun Chen, Cheng Su, Dan Protein Sci Full‐Length Papers The pandemic outbreak of coronavirus disease 2019 (COVID‐19) across the world has led to millions of infection cases and caused a global public health crisis. Current research suggests that SARS‐CoV‐2 is a highly contagious coronavirus that spreads rapidly through communities. To understand the mechanisms of viral replication, it is imperative to investigate coronavirus viral replicase, a huge protein complex comprising up to 16 viral nonstructural and associated host proteins, which is the most promising antiviral target for inhibiting viral genome replication and transcription. Recently, several components of the viral replicase complex in SARS‐CoV‐2 have been solved to provide a basis for the design of new antiviral therapeutics. Here, we report the crystal structure of the SARS‐CoV‐2 nsp7+8 tetramer, which comprises two copies of each protein representing nsp7's full‐length and the C‐terminus of nsp8 owing to N‐terminus proteolysis during the process of crystallization. We also identified a long helical extension and highly flexible N‐terminal domain of nsp8, which is preferred for interacting with single‐stranded nucleic acids. John Wiley & Sons, Inc. 2021-02-25 2021-04 /pmc/articles/PMC7980517/ /pubmed/33594727 http://dx.doi.org/10.1002/pro.4046 Text en © 2021 The Protein Society.
spellingShingle Full‐Length Papers
Zhang, Changhui
Li, Li
He, Jun
Chen, Cheng
Su, Dan
Nonstructural protein 7 and 8 complexes of SARS‐CoV‐2
title Nonstructural protein 7 and 8 complexes of SARS‐CoV‐2
title_full Nonstructural protein 7 and 8 complexes of SARS‐CoV‐2
title_fullStr Nonstructural protein 7 and 8 complexes of SARS‐CoV‐2
title_full_unstemmed Nonstructural protein 7 and 8 complexes of SARS‐CoV‐2
title_short Nonstructural protein 7 and 8 complexes of SARS‐CoV‐2
title_sort nonstructural protein 7 and 8 complexes of sars‐cov‐2
topic Full‐Length Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7980517/
https://www.ncbi.nlm.nih.gov/pubmed/33594727
http://dx.doi.org/10.1002/pro.4046
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