Science Daily July 21, 2021
A strategy to develop broad-spectrum inhibitors is to pharmacologically target binding sites on SARS-CoV-2 proteins that are highly conserved in other known coronaviruses, the assumption being that any selective pressure to keep a site conserved across past viruses will apply to future ones. An international team of researchers (Canada, UK) systematically mapped druggable binding pockets on the experimental structure of 15 SARS-CoV-2 proteins and analyzed their variation across 27 α- and β-coronaviruses and across thousands of SARS-CoV-2 samples from COVID-19 patients. They found that the two most conserved druggable sites are a pocket overlapping the RNA binding site of the helicase nsp13 and the catalytic site of the RNA-dependent RNA polymerase nsp12, both components of the viral replication–transcription complex. They have made the data available on a public web portal where users can interactively navigate individual protein structures and view the genetic variability of drug-binding pockets in 3D…read more. Open Access TECHNICAL ARTICLEÂ
Abstract. Credit: J. Proteome Res. 2021, XXXX, XXX, XXX-XXX, June 28, 2021