About: Structural basis of RNA recognition by the SARS-CoV-2 nucleocapsid phosphoprotein

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Structural basis of RNA recognition by the SARS-CoV-2 nucleocapsid phosphoprotein Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Structural basis of RNA recognition by the SARS-CoV-2 nucleocapsid phosphoprotein
Creator	Boura, Evzen Chalupska, Dominika Chandrasekaran, Dhurvas Silhan, Jan Veverka, Vaclav
Source	BioRxiv
abstract	Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of the Coronavirus disease 2019 (COVID-19) which is currently negatively affecting the population and disrupting the global economy. SARS-CoV-2 belongs to the +RNA virus family that utilize single-stranded positive-sense RNA molecules as genomes. SARS-CoV-2, like other coronaviruses, has an unusually large genome for a +RNA virus that encodes four structural proteins – the matrix (M), small envelope (E), spike (S) and nucleocapsid phosphoprotein (N) - and sixteen nonstructural proteins (nsp1-16) that together ensure replication of the virus in the host cell. The nucleocapsid phosphoprotein N is essential for linking the viral genome to the viral membrane. Its N-terminal RNA binding domain (N-NTD) captures the RNA genome while the C-terminal domain anchors the ribonucleoprotein complex to the viral membrane via its interaction with the M protein. Here, we characterized the structure of the N-NTD and its interaction with RNA using NMR spectroscopy. We observed a positively charged canyon on the surface of the N-NTD lined with arginine residues suggesting a putative RNA binding site. Next, we performed an NMR titration experiment using an RNA duplex. The observed changes in positions of signals in the N-NTD NMR spectra allowed us to construct a model of the N-NTD in complex with RNA.
has issue date	2020-04-05(xsd:dateTime)
bibo:doi	10.1101/2020.04.02.022194
has license	biorxiv
sha1sum (hex)	fd41cb24c85da1cc2af6230f04763de28fd2b39f
schema:url	https://doi.org/10.1101/2020.04.02.022194
resource representing a document's title	Structural basis of RNA recognition by the SARS-CoV-2 nucleocapsid phosphoprotein
schema:publication	bioRxiv
resource representing a document's body	covid:fd41cb24c85da1cc2af6230f04763de28fd2b39f#body_text
is schema:about of	named entity 'RNA virus' named entity 'replication' named entity 'genome' named entity 'essential' named entity 'ensure' named entity 'RNA GENOME' named entity 'SMALL' named entity 'POSITIVE' named entity '28S' named entity 'ENSURE' named entity 'RNA' named entity 'CURRENTLY' named entity 'linking' named entity 'RNA virus' named entity 'RNA' named entity 'genomes' named entity 'genome' named entity 'viral genome' named entity 'virus' named entity 'protein' named entity 'nonstructural proteins' named entity 'N-terminal' named entity 'RNA' named entity 'T57' named entity 'remdesivir' named entity 'YASARA' named entity 'crystal lattice' named entity 'β-hairpin' named entity 'RNA' named entity 'PyMOL' named entity 'China' named entity 'RNA' named entity 'R107' named entity 'favipiravir' named entity 'double-stranded RNA' named entity 'SARS-CoV-2' named entity 'protein' named entity 'protein' named entity 'protein' named entity 'molecule' named entity 'protein' named entity 'crystal structure' named entity 'NOE' named entity 'severe acute respiratory syndrome coronavirus 2' named entity 'RNA' named entity 'T57' named entity 'protein NMR' named entity 'protein' named entity 'COVID' named entity 'NMR spectroscopy' named entity 'virus' named entity 'nucleotide analogs' named entity 'unliganded' named entity 'SARS-CoV-2' named entity 'protein' named entity 'HMQC' named entity 'triple-resonance' named entity 'NOE' named entity 'homology model' named entity 'protein' named entity 'A90' named entity 'Viral' named entity 'human health' named entity 'innate immunity' named entity 'electrostatic potential' named entity 'exonuclease' named entity 'RNA' named entity 'protein' named entity 'RNA replication' named entity 'phosphoprotein' named entity 'MERS' named entity 'antiviral' named entity 'SARS-CoV-2' named entity 'viruses' named entity 'electrostatic potential' named entity 'R149' named entity 'protein' named entity 'β-sheet' named entity 'YASARA' named entity 'RNA genome'

Faceted Search & Find service v1.13.91 as of Mar 24 2020

Alternative Linked Data Documents: Sponger | ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2025 OpenLink Software