tetano
Editor, Senior Moderator
J Mol Graph Model
. 2022 Jan 5;112:108122.
doi: 10.1016/j.jmgm.2022.108122. Online ahead of print.
Molecular dynamics simulations of the flexibility and inhibition of SARS-CoV-2 NSP 13 helicase
Bryan A Raubenolt[SUP] 1 [/SUP], Naeyma N Islam[SUP] 1 [/SUP], Christoper M Summa[SUP] 2 [/SUP], Steven W Rick[SUP] 3 [/SUP]
Affiliations
Abstract
The helicase protein of the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) is both a good potential drug target and very flexible. The flexibility, and therefore its function, could be reduced through knowledge of these motions and identification of allosteric pockets. Using molecular dynamics simulations with enhanced sampling, we determined key modes of motion and sites on the protein that are at the interface between flexible domains of the proteins. We developed an approach to map the principal components of motion onto the surface of a potential binding pocket to help in the identification of allosteric sites.
. 2022 Jan 5;112:108122.
doi: 10.1016/j.jmgm.2022.108122. Online ahead of print.
Molecular dynamics simulations of the flexibility and inhibition of SARS-CoV-2 NSP 13 helicase
Bryan A Raubenolt[SUP] 1 [/SUP], Naeyma N Islam[SUP] 1 [/SUP], Christoper M Summa[SUP] 2 [/SUP], Steven W Rick[SUP] 3 [/SUP]
Affiliations
- PMID: 35021142
- DOI: 10.1016/j.jmgm.2022.108122
Abstract
The helicase protein of the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) is both a good potential drug target and very flexible. The flexibility, and therefore its function, could be reduced through knowledge of these motions and identification of allosteric pockets. Using molecular dynamics simulations with enhanced sampling, we determined key modes of motion and sites on the protein that are at the interface between flexible domains of the proteins. We developed an approach to map the principal components of motion onto the surface of a potential binding pocket to help in the identification of allosteric sites.