Journal
CHEMICAL COMMUNICATIONS
Volume 57, Issue 64, Pages 7910-7913Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d1cc02956h
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Funding
- H2020 -INFRAIA iNEXT-Discovery -Structural Biology Research Infrastructures for Translational Research and Discovery [871037]
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This study elucidated the structural basis of ionic zinc binding to the SARS-CoV-2 main protease using X-ray crystallography. The zinc binding affinity and its ability to inhibit the main protease were investigated, providing a solid foundation for the design of potent and selective metal-conjugated inhibitors.
Structural data on the SARS-CoV-2 main protease in complex with a zinc-containing organic inhibitor are already present in the literature and gave hints on the presence of a zinc binding site involving the catalytically relevant cysteine and histidine residues. In this paper, the structural basis of ionic zinc binding to the SARS-CoV-2 main protease has been elucidated by X-ray crystallography. The zinc binding affinity and its ability to inhibit the SARS-CoV-2 main protease have been investigated. These findings provide solid ground for the design of potent and selective metal-conjugated inhibitors of the SARS-CoV-2 main protease.
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