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Structural basis for SARS-CoV-2 nucleocapsid (N) protein recognition by 14-3-3 proteins
14-3-3 proteins are important dimeric scaffolds that regulate the function of hundreds of proteins in a phosphorylation-dependent manner. The SARS-CoV-2 nucleocapsid (N) protein forms a complex with human 14-3-3 proteins upon phosphorylation, which has also been described for other coronaviruses. He...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier Inc.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9245327/ https://www.ncbi.nlm.nih.gov/pubmed/35781025 http://dx.doi.org/10.1016/j.jsb.2022.107879 |
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author | Eisenreichova, Andrea Boura, Evzen |
author_facet | Eisenreichova, Andrea Boura, Evzen |
author_sort | Eisenreichova, Andrea |
collection | PubMed |
description | 14-3-3 proteins are important dimeric scaffolds that regulate the function of hundreds of proteins in a phosphorylation-dependent manner. The SARS-CoV-2 nucleocapsid (N) protein forms a complex with human 14-3-3 proteins upon phosphorylation, which has also been described for other coronaviruses. Here, we report a high-resolution crystal structure of 14-3-3 bound to an N phosphopeptide bearing the phosphoserine 197 in the middle. The structure revealed two copies of the N phosphopeptide bound, each in the central binding groove of each 14-3-3 monomer. A complex network of hydrogen bonds and water bridges between the peptide and 14-3-3 was observed explaining the high affinity of the N protein for 14-3-3 proteins. |
format | Online Article Text |
id | pubmed-9245327 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Elsevier Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-92453272022-07-01 Structural basis for SARS-CoV-2 nucleocapsid (N) protein recognition by 14-3-3 proteins Eisenreichova, Andrea Boura, Evzen J Struct Biol Article 14-3-3 proteins are important dimeric scaffolds that regulate the function of hundreds of proteins in a phosphorylation-dependent manner. The SARS-CoV-2 nucleocapsid (N) protein forms a complex with human 14-3-3 proteins upon phosphorylation, which has also been described for other coronaviruses. Here, we report a high-resolution crystal structure of 14-3-3 bound to an N phosphopeptide bearing the phosphoserine 197 in the middle. The structure revealed two copies of the N phosphopeptide bound, each in the central binding groove of each 14-3-3 monomer. A complex network of hydrogen bonds and water bridges between the peptide and 14-3-3 was observed explaining the high affinity of the N protein for 14-3-3 proteins. Elsevier Inc. 2022-09 2022-06-30 /pmc/articles/PMC9245327/ /pubmed/35781025 http://dx.doi.org/10.1016/j.jsb.2022.107879 Text en © 2022 Elsevier Inc. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
spellingShingle | Article Eisenreichova, Andrea Boura, Evzen Structural basis for SARS-CoV-2 nucleocapsid (N) protein recognition by 14-3-3 proteins |
title | Structural basis for SARS-CoV-2 nucleocapsid (N) protein recognition by 14-3-3 proteins |
title_full | Structural basis for SARS-CoV-2 nucleocapsid (N) protein recognition by 14-3-3 proteins |
title_fullStr | Structural basis for SARS-CoV-2 nucleocapsid (N) protein recognition by 14-3-3 proteins |
title_full_unstemmed | Structural basis for SARS-CoV-2 nucleocapsid (N) protein recognition by 14-3-3 proteins |
title_short | Structural basis for SARS-CoV-2 nucleocapsid (N) protein recognition by 14-3-3 proteins |
title_sort | structural basis for sars-cov-2 nucleocapsid (n) protein recognition by 14-3-3 proteins |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9245327/ https://www.ncbi.nlm.nih.gov/pubmed/35781025 http://dx.doi.org/10.1016/j.jsb.2022.107879 |
work_keys_str_mv | AT eisenreichovaandrea structuralbasisforsarscov2nucleocapsidnproteinrecognitionby1433proteins AT bouraevzen structuralbasisforsarscov2nucleocapsidnproteinrecognitionby1433proteins |