SARS-COV-2 Mpro conformational changes induced by covalently bound ligand
| Autor: | Ferreira, G. M., Kronenberger, T, Arun Kumar Tonduru, Hirata, R. D. C., Hirata, M.H., Poso, A. |
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| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: | |
| DOI: | 10.5281/zenodo.3980659 |
| Popis: | Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has been identified as the etiologic agent of COVID-19 (Coronavirus Disease 2019) and is responsible for the 2019 – 2020’s viral pneumonia outbreak started in Wuhan (China). Currently, increase the search for a new compound satisfactory against SARS-CoV-2. Therefore, there is still a very wide field for the search for new small molecules as drug candidates for effective treatment. SARS-CoV-2 main protease (Mpro) plays a crucial role in processing the polyprotein into mature proteins, making it a relevant target for drug discovery, despite its high flexibility. Recently, several SARS-CoV-2 Mpro structures co-crystallized with different ligands became available, however little diversity has been observed in the protein conformation. In this sense, this work discusses the influence of ligand binding in the SARS-CoV-2 Mpro dynamics and the inhibitory mechanism using molecular dynamics simulation. We hope that bridging the gap between the static crystals and the protein dynamics one can discover new small molecules inhibitors for COVID-19 treatment. The files include raw trajectory files of the Desmond MD simulations of different Mpro inhibitors and apostructures. (trajectory format is out.cms and the full trj files, Schrödinger, LLC, New York, NY, 2019, more details on the materials and methods section of the respective publication). São Paulo research foundation (FAPESP - 2019/24112-9) |
| Databáze: | OpenAIRE |
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