Document Type
Article
Publication Date
2022
Keywords
Sars-cov-2 Main Protease, Dynamics, Replica Exchange MD Simulations
Digital Object Identifier (DOI)
https://doi.org/10.1016/j.crstbi.2022.11.001
Abstract
SARS-CoV-2 is the infectious agent responsible for the coronavirus disease since 2019, which is the viral pneumonia pandemic worldwide. The structural knowledge on SARS-CoV-2 is rather limited. These limitations are also applicable to one of the most attractive drug targets of SARS-CoV-2 proteins – namely, main protease Mpro, also known as 3C-like protease (3CLpro). This protein is crucial for the processing of the viral polyproteins and plays crucial roles in interfering viral replication and transcription. In fact, although the crystal structure of this protein with an inhibitor was solved, Mpro conformational dynamics in aqueous solution is usually studied by molecular dynamics simulations without special sampling techniques. We conducted replica exchange molecular dynamics simulations on Mpro in water and report the dynamic structures of Mpro in an aqueous environment including root mean square fluctuations, secondary structure properties, radius of gyration, and end-to-end distances, chemical shift values, intrinsic disorder characteristics of Mpro and its active sites with a set of computational tools. The active sites we found coincide with the currently known sites and include a new interface for interaction with a protein partner.
Rights Information
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Current Research in Structural Biology, v. 4, p. 349-355
Scholar Commons Citation
Akbaryak, Ibrahim Y.; Caglayan, Sule I.; Kurgan, Lukasz; Uversky, Vladimir N.; and Coskuner-Weber, Orkid, "Insights Into the Structural Properties of SARS-CoV-2 Main Protease" (2022). Molecular Medicine Faculty Publications. 1047.
https://digitalcommons.usf.edu/mme_facpub/1047
