About: The Discovery of a Putative Allosteric Site in the SARS-CoV-2 Spike Protein Using an Integrated Structural/Dynamic Approach

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

About: The Discovery of a Putative Allosteric Site in the SARS-CoV-2 Spike Protein Using an Integrated Structural/Dynamic Approach Goto Sponge NotDistinct Permalink

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	The Discovery of a Putative Allosteric Site in the SARS-CoV-2 Spike Protein Using an Integrated Structural/Dynamic Approach
Creator	Giuliani, Alessandro Hadi-Alijanvand, Hamid Hu, Guang Paola, Luisa Song, Xingyu
topic	covid:916aee323d34764317d7662a6aae52c079686741#this
Source	Medline; PMC
abstract	[Image: see text] SARS-CoV-2 has caused the largest pandemic of the twenty-first century (COVID-19), threatening the life and economy of all countries in the world. The identification of novel therapies and vaccines that can mitigate or control this global health threat is among the most important challenges facing biomedical sciences. To construct a long-term strategy to fight both SARS-CoV-2 and other possible future threats from coronaviruses, it is critical to understand the molecular mechanisms underlying the virus action. The viral entry and associated infectivity stems from the formation of the SARS-CoV-2 spike protein complex with angiotensin-converting enzyme 2 (ACE2). The detection of putative allosteric sites on the viral spike protein molecule can be used to elucidate the molecular pathways that can be targeted with allosteric drugs to weaken the spike-ACE2 interaction and, thus, reduce viral infectivity. In this study, we present the results of the application of different computational methods aimed at detecting allosteric sites on the SARS-CoV-2 spike protein. The adopted tools consisted of the protein contact networks (PCNs), SEPAS (Affinity by Flexibility), and perturbation response scanning (PRS) based on elastic network modes. All of these methods were applied to the ACE2 complex with both the SARS-CoV2 and SARS-CoV spike proteins. All of the adopted analyses converged toward a specific region (allosteric modulation region [AMR]), present in both complexes and predicted to act as an allosteric site modulating the binding of the spike protein with ACE2. Preliminary results on hepcidin (a molecule with strong structural and sequence with AMR) indicated an inhibitory effect on the binding affinity of the spike protein toward the ACE2 protein.
has issue date	2020-06-17(xsd:dateTime)
bibo:doi	10.1021/acs.jproteome.0c00273
bibo:pmid	32551648
has license	no-cc
sha1sum (hex)	916aee323d34764317d7662a6aae52c079686741
schema:url	https://doi.org/10.1021/acs.jproteome.0c00273
resource representing a document's title	The Discovery of a Putative Allosteric Site in the SARS-CoV-2 Spike Protein Using an Integrated Structural/Dynamic Approach
has PubMed Central identifier	PMC7331933
has PubMed identifier	32551648
schema:publication	J Proteome Res
resource representing a document's body	covid:916aee323d34764317d7662a6aae52c079686741#body_text
is http://vocab.deri.ie/void#inDataset of	https://covidontheweb.inria.fr:4443/about/id/http/ns.inria.fr/covid19/916aee323d34764317d7662a6aae52c079686741
is schema:about of	named entity 'structural' named entity 'molecule' named entity 'protein' named entity 'The' named entity 'sites' named entity 'computational' named entity 'action' named entity 'spike' named entity 'therapies' named entity 'facing' named entity 'construct' named entity 'vaccines' named entity 'viral entry' named entity 'drugs' named entity 'The' named entity 'angiotensin-converting enzyme 2' named entity 'region' named entity 'ACE2' named entity 'ACE2' named entity 'twenty-first' named entity 'allosteric' named entity 'predicted' named entity 'ACE2' named entity 'Structural' named entity 'SARS-CoV-2' named entity 'spike protein' named entity 'ACE2' named entity 'infectivity' named entity 'hepcidin' named entity 'molecule' named entity 'SARS-CoV-2' named entity 'ACE2' named entity 'SARS-CoV-2' named entity 'eigenvector' named entity 'RBDs' named entity 'GNM' named entity 'virus' named entity 'vector' named entity 'SARS-CoV' named entity 'RBDs' named entity 'high affinity' named entity 'SARS-CoV-2' named entity 'protein complexes' named entity 'binding affinity' named entity 'gastrointestinal' named entity 'ACE2' named entity 'fusion peptide' named entity 'Spectral clustering' named entity 'locus' named entity 'SARS-CoV' named entity 'SARS-CoV-2' named entity 'cytokine storm' named entity 'SARS' named entity 'infection' named entity 'potential energy' named entity 'SARS-CoV' named entity 'ligand' named entity 'SARS-CoV-2' named entity 'peptides' named entity 'SARS-CoV-2' named entity 'ACE2' named entity 'eigenvalue decomposition' named entity 'SARS-CoV-2' named entity 'molecular basis' named entity 'ANM' named entity 'ACE2' named entity 'binding site' named entity 'ABC' named entity 'ACE2' named entity 'force constant' named entity 'viral entry' named entity 'SARS' named entity 'SARS-CoV-2' named entity 'PDF' named entity 'spike proteins'

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 © 2009-2024 OpenLink Software