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Dynamics and electrostatics define an allosteric druggable site within the receptor-binding domain of SARS-CoV-2 spike protein

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Title Dynamics and electrostatics define an allosteric druggable
site within the receptor-binding domain of SARS-CoV-2
spike protein
 
Creator Bhattacharjee, Sayan
Bhattacharyya, Rajanya
Sengupta, Jayati
 
Subject Structural Biology & Bioinformatics
 
Description The pathogenesis of the SARS-CoV-2 virus initiates through recognition of
the angiotensin-converting enzyme 2 (ACE2) receptor of the host cells by the
receptor-binding domain (RBD) located at the spikes of the virus. Here, using
molecular dynamics simulations, we have demonstrated the allosteric crosstalk within the RBD in the apo- and the ACE2 receptor-bound states, revealing the contribution of the dynamics-based correlated motions and the
electrostatic energy perturbations to this crosstalk. While allostery, based on
correlated motions, dominates inherent distal communication in the apoRBD, the electrostatic energy perturbations determine favorable pairwise
crosstalk within the RBD residues upon binding to ACE2. Interestingly, the
allosteric path is composed of residues which are evolutionarily conserved
within closely related coronaviruses, pointing toward the biological relevance
of the communication and its potential as a target for drug development.
 
Publisher Elsevier
 
Date 2021
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/2820/1/1873%2D3468.14038.pdf
Bhattacharjee, Sayan and Bhattacharyya, Rajanya and Sengupta, Jayati (2021) Dynamics and electrostatics define an allosteric druggable site within the receptor-binding domain of SARS-CoV-2 spike protein. FEBS Letters.
 
Relation http://www.eprints.iicb.res.in/2820/