PMC:7210460 / 746-1837 JSONTXT

{"target":"http://pubannotation.org/docs/sourcedb/PMC/sourceid/7210460","sourcedb":"PMC","sourceid":"7210460","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7210460","text":"An outbreak of series of acute respiratory illness caused by a novel coronavirus, SARS-CoV-2, caused a global threat in 20202. The world health organization (WHO) named the disease “COVID-19” and declared it as a world health emergency pandemic. Studying the crystal structure of targets for treatment is very crucial to know the mechanism of action of prospective drugs. A structural study on the coronavirus main protease 3CLpro inhibitor complex established designing of broad-spectrum halomethyl ketone inhibitors to the Coronaviridae family and demonstrated that these inhibitors form a thioether linkage with high affinity to the target3. Hilgenfeld’s group reported earlier that a structure-based design of peptidomimetic α-ketoamides are also effective broad-spectrum inhibitors to the main and 3C protease of coronaviruses and enteroviruses as demonstrated by crystal structure of inhibitor-protease complex4. The 3CL protease of coronaviruses facilitates viral assembly by cleaving polyproteins and most active compounds prevent disease progression by inhibiting viral proteases 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