PMC:7291971 / 1088-1635 JSONTXT

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{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7291971","sourcedb":"PMC","sourceid":"7291971","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7291971","text":"unds were barely active against 2′-O MTases of several flaviviruses or SARS-CoV but surprisingly, seven of them showed efficient and specific inhibition against SARS-CoV N7-MTase (nsp14) in the micromolar to submicromolar range. The most active nsp14 inhibitor identified is as potent as but particularly more specific than the broad-spectrum MTase inhibitor, sinefungin. Molecular docking suggests that the inhibitor binds to a pocket formed by the S-adenosyl methionine (SAM) and cap RNA binding sites, conserved among SARS-CoV nsp14. 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