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Analyzing 3D structures of the SARS-CoV-2 main protease reveals structural features of ligand binding for COVID-19 drug discovery

Material type: TextSeries: ; Drug Discovery Today, 28(10), p.103727, 2023Contained works:
  • Xu, L
  • Chen, R
  • Liu, J
  • Patterson, T. A
  • Hong, H
Subject(s): Online resources: Abstract: The severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2)main protease has an essential role in viral replication and has become a major target for coronavirus 2019 (COVID-19)drug development. Various inhibitors have been discovered or designed to bind to the main protease. The availability of more than 550 3D structures of the main protease provides a wealth of structural details on the main protease in both ligand-free and ligand-bound states. Therefore, we examined these structures to ascertain the structural features for the role of the main protease in the cleavage of polyproteins, the alternative conformations during main protease maturation, and ligand interactions in the main protease. The structural features unearthed could promote the development of COVID-19 drugs targeting the SARS-CoV-2 main protease.
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The severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2)main protease has an essential role in viral replication and has become a major target for coronavirus 2019 (COVID-19)drug development. Various inhibitors have been discovered or designed to bind to the main protease. The availability of more than 550 3D structures of the main protease provides a wealth of structural details on the main protease in both ligand-free and ligand-bound states. Therefore, we examined these structures to ascertain the structural features for the role of the main protease in the cleavage of polyproteins, the alternative conformations during main protease maturation, and ligand interactions in the main protease. The structural features unearthed could promote the development of COVID-19 drugs targeting the SARS-CoV-2 main protease.

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