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?:abstract
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There is an urgent necessity of effective medication against severe acute respiratory syndrome coronavirus 2 (SARS CoV-2), which is producing the COVID-19 pandemic across the world. Its main protease (M [Formula: see text]) represents an attractive pharmacological target due to its involvement in essential viral functions. The crystal structure of free M [Formula: see text] shows a large structural resemblance with the main protease of SARS CoV (nowadays known as SARS CoV-1). Here, we report that average SARS CoV-2 M [Formula: see text] is 1900% more sensitive than SARS CoV-1 M [Formula: see text] in transmitting tiny structural changes across the whole protein through long-range interactions. The largest sensitivity of M [Formula: see text] to structural perturbations is located exactly around the catalytic site Cys-145 and coincides with the binding site of strong inhibitors. These findings, based on a simplified representation of the protein as a residue network, may help in designing potent inhibitors of SARS CoV-2 M [Formula: see text].
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document_parses/pdf_json/84590ca5cb157053a2d944aa84f361c4f00dd801.json
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document_parses/pmc_json/PMC7286701.xml.json
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?:title
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Topological analysis of SARS CoV-2 main protease
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