The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1–248 residue construct: sequence-specific resonance assignments through NMR

The nucleocapsid protein N from SARS-CoV-2 is one of the most highly expressed proteins by the virus and plays a number of important roles in the transcription and assembly of the virion within the infected host cell. It is expected to be characterized by a highly dynamic and heterogeneous structure...

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Autores principales: Schiavina, Marco, Pontoriero, Letizia, Uversky, Vladimir N., Felli, Isabella C., Pierattelli, Roberta
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2021
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7928198/
https://www.ncbi.nlm.nih.gov/pubmed/33660218
http://dx.doi.org/10.1007/s12104-021-10009-8
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author Schiavina, Marco
Pontoriero, Letizia
Uversky, Vladimir N.
Felli, Isabella C.
Pierattelli, Roberta
author_facet Schiavina, Marco
Pontoriero, Letizia
Uversky, Vladimir N.
Felli, Isabella C.
Pierattelli, Roberta
author_sort Schiavina, Marco
collection PubMed
description The nucleocapsid protein N from SARS-CoV-2 is one of the most highly expressed proteins by the virus and plays a number of important roles in the transcription and assembly of the virion within the infected host cell. It is expected to be characterized by a highly dynamic and heterogeneous structure as can be inferred by bioinformatics analyses as well as from the data available for the homologous protein from SARS-CoV. The two globular domains of the protein (NTD and CTD) have been investigated while no high-resolution information is available yet for the flexible regions of the protein. We focus here on the 1–248 construct which comprises two disordered fragments (IDR1 and IDR2) in addition to the N-terminal globular domain (NTD) and report the sequence-specific assignment of the two disordered regions, a step forward towards the complete characterization of the whole protein.
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spelling pubmed-79281982021-03-04 The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1–248 residue construct: sequence-specific resonance assignments through NMR Schiavina, Marco Pontoriero, Letizia Uversky, Vladimir N. Felli, Isabella C. Pierattelli, Roberta Biomol NMR Assign Article The nucleocapsid protein N from SARS-CoV-2 is one of the most highly expressed proteins by the virus and plays a number of important roles in the transcription and assembly of the virion within the infected host cell. It is expected to be characterized by a highly dynamic and heterogeneous structure as can be inferred by bioinformatics analyses as well as from the data available for the homologous protein from SARS-CoV. The two globular domains of the protein (NTD and CTD) have been investigated while no high-resolution information is available yet for the flexible regions of the protein. We focus here on the 1–248 construct which comprises two disordered fragments (IDR1 and IDR2) in addition to the N-terminal globular domain (NTD) and report the sequence-specific assignment of the two disordered regions, a step forward towards the complete characterization of the whole protein. Springer Netherlands 2021-03-03 2021 /pmc/articles/PMC7928198/ /pubmed/33660218 http://dx.doi.org/10.1007/s12104-021-10009-8 Text en © The Author(s) 2021 Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Schiavina, Marco
Pontoriero, Letizia
Uversky, Vladimir N.
Felli, Isabella C.
Pierattelli, Roberta
The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1–248 residue construct: sequence-specific resonance assignments through NMR
title The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1–248 residue construct: sequence-specific resonance assignments through NMR
title_full The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1–248 residue construct: sequence-specific resonance assignments through NMR
title_fullStr The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1–248 residue construct: sequence-specific resonance assignments through NMR
title_full_unstemmed The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1–248 residue construct: sequence-specific resonance assignments through NMR
title_short The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1–248 residue construct: sequence-specific resonance assignments through NMR
title_sort highly flexible disordered regions of the sars-cov-2 nucleocapsid n protein within the 1–248 residue construct: sequence-specific resonance assignments through nmr
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7928198/
https://www.ncbi.nlm.nih.gov/pubmed/33660218
http://dx.doi.org/10.1007/s12104-021-10009-8
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