A detailed understanding of SARS-CoV-2 structure brings new possibilities in drug design and rises a chance to successfully combat the pandemic. The SARS-CoV-2 belongs to the +RNA family and its unusually large genome (29.8 kb) encodes four structural proteins together with other sixteen non-structural proteins.
Researchers from IOCB Prague led by Václav Veverka and Evžen Bouřa studied the nucleocapsid phosphoprotein (N), which is one of the structural proteins and its function is linking the +RNA strain with the viral envelope.
The scientists analyzed in-depth the structure of the N protein and its interaction with RNA using NMR. They discovered a large and highly positively charged groove on the surface of one of the N protein domains, which was confirmed to be an RNA binding site. The experimental data from RNA recognition together with the results from the structural analysis are strengthened by computer simulations.
The RNA-binding groove can serve as a target for novel inhibitors of RNA-protein interaction, which could be used together with other compounds in highly active antiretroviral therapy.
Read the paper:
- Dinesh DC, Chalupska D, Silhan J, Koutna E, Nencka R, Veverka V, Boura E (2020) Structural basis of RNA recognition by the SARS-CoV-2 nucleocapsid phosphoprotein. PLOS Pathogens 16(12): e1009100. https://doi.org/10.1371/journal.ppat.1009100
