Link to bioRxiv paper: http://biorxiv.org/cgi/content/short/2020.11.03.366609v1?rss=1 Authors: Berta, D., Badaoui, M., Buigues, P. J., Martino, S. A., Pisliakov, A., Elghobashi-Meinhardt, N., Wells, G., Harris, S. A., Frezza, E., Rosta, E. Abstract: Having claimed over 1 million lives worldwide to date, the ongoing COVID-19 pandemic has created one of the biggest challenges to develop an effective drug to treat infected patients. Among all the proteins expressed by the virus, RNA helicase is a fundamental protein for viral replication, and it is highly conserved among the coronaviridae family. To date, there is no high-resolution structure of helicase bound with ATP and RNA. We present here structural insights and molecular dynamics (MD) simulation results of the SARS-CoV-2 RNA helicase both in its apo form and in complex with its natural substrates. Our structural information of the catalytically competent helicase complex provides valuable insights for the mechanism and function of this enzyme at the atomic level, a key to develop specific inhibitors for this potential COVID-19 drug target. Copy rights belong to original authors. Visit the link for more info