About: Structural Insights into the mechanism of RNA recognition by the N-terminal RNA-binding domain of the SARS-CoV-2 nucleocapsid phosphoprotein

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

About: Structural Insights into the mechanism of RNA recognition by the N-terminal RNA-binding domain of 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
title	Structural Insights into the mechanism of RNA recognition by the N-terminal RNA-binding domain of the SARS-CoV-2 nucleocapsid phosphoprotein
Creator	Wei, Dong-Qing Khan, Muhammad Ali, A Khan, M Khan, Mazhar Tahir, Muhammad Wei, Khan, A Syed, Ali, Arif Ali, Mazhar Ali, Shujait Junaid, M Junaid, Muhammad Khan, Abbas Khan, Dong-Qing Saleem, S Saleem, Shoaib Shujait, S Syed, Shujait Wei, D-Q
source	Elsevier; Medline; PMC
abstract	The emergence of recent SARS-CoV-2 has become a global health issue. This single-stranded positive-sense RNA virus is continuously spreading with increasing morbidities and mortalities. The proteome of this virus contains four structural and sixteen nonstructural proteins that ensure the replication of the virus in the host cell. However, the role of phosphoprotein (N) in RNA recognition, replicating, transcribing the viral genome, and modulating the host immune response is indispensable. Recently, the NMR structure of the N-terminal domain of the Nucleocapsid Phosphoprotein has been reported, but its precise structural mechanism of how the ssRNA interacts with it is not reported yet. Therefore, here, we have used an integrated computational pipeline to identify the key residues, which play an essential role in RNA recognition. We generated multiple variants by using an alanine scanning strategy and performed an extensive simulation for each system to signify the role of each interfacial residue. Our analyses suggest that residues T57A, H59A, S105A, R107A, F171A, and Y172A significantly affected the dynamics and binding of RNA. Furthermore, per-residue energy decomposition analysis suggests that residues T57, H59, S105 and R107 are the key hotspots for drug discovery. Thus, these residues may be useful as potential pharmacophores in drug designing.
has issue date	2020-08-12(xsd:dateTime)
bibo:doi	10.1016/j.csbj.2020.08.006
bibo:pmid	32837710
has license	no-cc
sha1sum (hex)	039ea9cc12ba41a6a233ee921a9f2d7649408522
schema:url	https://doi.org/10.1016/j.csbj.2020.08.006
resource representing a document's title	Structural Insights into the mechanism of RNA recognition by the N-terminal RNA-binding domain of the SARS-CoV-2 nucleocapsid phosphoprotein
has PubMed Central identifier	PMC7419326
has PubMed identifier	32837710
schema:publication	Comput Struct Biotechnol J
resource representing a document's body	covid:039ea9cc12ba41a6a233ee921a9f2d7649408522#body_text
is schema:about of	named entity 'virus' named entity 'replicating' named entity 'precise' named entity 'host' named entity 'performed' named entity 'emergence' named entity 'nucleocapsid' named entity 'domain' named entity 'Journal' named entity 'MULTIPLE' named entity 'GENERATED' named entity 'REPLICATION' named entity 'KEY' named entity 'PROTEOME' named entity 'INCREASING' named entity 'USED' named entity 'Therefore' named entity 'structural' named entity 'nonstructural proteins' named entity 'key' named entity 'key' named entity 'R107' named entity 'continuously' named entity 'RNA virus' named entity 'structure' named entity 'proteome' named entity 'Phosphoprotein' named entity 'signify' named entity 'Our' named entity 'Structural' named entity 'ssRNA' named entity 'proteome' named entity 'N-terminal domain' named entity 'virus' named entity 'positive-sense RNA' named entity 'NMR' named entity 'R107' named entity 'RNA' named entity 'Nucleocapsid' named entity 'single-stranded' named entity 'N-terminal' named entity 'phosphoprotein' named entity 'nucleocapsid' named entity 'RNA' named entity 'N-terminal' named entity 'protein' named entity 'antiviral drug' named entity 'spike proteins' named entity '3D structure' named entity 'β-hairpin' named entity 'coronaviruses' named entity 'phosphoprotein' named entity 'apoptosis' named entity 'RNA' named entity 'virus' named entity 'structural proteins' named entity 'wild type' named entity 'bioactivity' named entity 'mRNA' named entity 'R107' named entity 'protein'

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