This project is studying the NSP10 (Non-structural-protein-10) of SARS-CoV-2!
In this project we are analyzing the role of _every_ single residue in NSP10 using a computational mutagenesis approach. Each RUN in this project is simulating a unique mutant of NSP10, which we will compare to one another to identify critical residues of importance for NSP10 function.
NSP10 is an "activator" protein for critical viral function. Two other proteins, NSP14, and NSP16 are important enzymes for viral function, but they both require NSP10 to bind them and "activate" them. Without NSP10, these two enzymes would not function which would inhibit the virus from being able to replicate and transmit the infection COVID19. This makes NSP10 an interesting potential biological target, as blocking its role as an activator could provide a therapeutic opportunity.
However, it only participates in protein-protein interactions and does not have any obvious "pockets" or grooves amenable to targeting by drug design methods. We are simulating NSP10 to identify potential druggable sites that have not been previously observed using experimental studies. From a basic research standpoint, it will also be useful to understand how NSP10 actually "activates" its targets, as the mechanism of activation remains unknown.
List of Contributors
This project is managed by Sukrit Singh at Washington University in St. Louis.
Sukrit Singh is a Biophysics PhD student in Greg Bowman's lab at Washington University in St. Louis.
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