Flexibility and mobility of SARS-CoV-2-related protein structures

Abstract The worldwide CoVid-19 pandemic has led to an unprecedented push across the whole of the scientific community to develop a potent antiviral drug and vaccine as soon as possible. Existing academic, governmental and industrial institutions and companies have engaged in large-scale screening o...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Rudolf A. Römer, Navodya S. Römer, A. Katrine Wallis
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/688570778d83438cb05435cdff16ea03
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:688570778d83438cb05435cdff16ea03
record_format	dspace
spelling	oai:doaj.org-article:688570778d83438cb05435cdff16ea032021-12-02T14:03:45ZFlexibility and mobility of SARS-CoV-2-related protein structures10.1038/s41598-021-82849-22045-2322https://doaj.org/article/688570778d83438cb05435cdff16ea032021-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-82849-2https://doaj.org/toc/2045-2322Abstract The worldwide CoVid-19 pandemic has led to an unprecedented push across the whole of the scientific community to develop a potent antiviral drug and vaccine as soon as possible. Existing academic, governmental and industrial institutions and companies have engaged in large-scale screening of existing drugs, in vitro, in vivo and in silico. Here, we are using in silico modelling of possible SARS-CoV-2 drug targets, as deposited on the Protein Databank (PDB), and ascertain their dynamics, flexibility and rigidity. For example, for the SARS-CoV-2 spike protein—using its complete homo-trimer configuration with 2905 residues—our method identifies a large-scale opening and closing of the S1 subunit through movement of the S $${}^\text{B}$$ B domain. We compute the full structural information of this process, allowing for docking studies with possible drug structures. In a dedicated database, we present similarly detailed results for the further, nearly 300, thus far resolved SARS-CoV-2-related protein structures in the PDB.Rudolf A. RömerNavodya S. RömerA. Katrine WallisNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Rudolf A. Römer Navodya S. Römer A. Katrine Wallis Flexibility and mobility of SARS-CoV-2-related protein structures
description	Abstract The worldwide CoVid-19 pandemic has led to an unprecedented push across the whole of the scientific community to develop a potent antiviral drug and vaccine as soon as possible. Existing academic, governmental and industrial institutions and companies have engaged in large-scale screening of existing drugs, in vitro, in vivo and in silico. Here, we are using in silico modelling of possible SARS-CoV-2 drug targets, as deposited on the Protein Databank (PDB), and ascertain their dynamics, flexibility and rigidity. For example, for the SARS-CoV-2 spike protein—using its complete homo-trimer configuration with 2905 residues—our method identifies a large-scale opening and closing of the S1 subunit through movement of the S $${}^\text{B}$$ B domain. We compute the full structural information of this process, allowing for docking studies with possible drug structures. In a dedicated database, we present similarly detailed results for the further, nearly 300, thus far resolved SARS-CoV-2-related protein structures in the PDB.
format	article
author	Rudolf A. Römer Navodya S. Römer A. Katrine Wallis
author_facet	Rudolf A. Römer Navodya S. Römer A. Katrine Wallis
author_sort	Rudolf A. Römer
title	Flexibility and mobility of SARS-CoV-2-related protein structures
title_short	Flexibility and mobility of SARS-CoV-2-related protein structures
title_full	Flexibility and mobility of SARS-CoV-2-related protein structures
title_fullStr	Flexibility and mobility of SARS-CoV-2-related protein structures
title_full_unstemmed	Flexibility and mobility of SARS-CoV-2-related protein structures
title_sort	flexibility and mobility of sars-cov-2-related protein structures
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/688570778d83438cb05435cdff16ea03
work_keys_str_mv	AT rudolfaromer flexibilityandmobilityofsarscov2relatedproteinstructures AT navodyasromer flexibilityandmobilityofsarscov2relatedproteinstructures AT akatrinewallis flexibilityandmobilityofsarscov2relatedproteinstructures
_version_	1718392084522598400

Flexibility and mobility of SARS-CoV-2-related protein structures

Ejemplares similares