My goal is to look for strategies and chemical starting points to inhibit viral helicases, with a primary focus on the SARS-CoV-2 helicase NSP13. In a previous post, I showed that a binding pocket in the human helicase SNRNP200 exploited by an allosteric inhibitor (PDB code 5URK) was absent in SARS-CoV-2. Here, I analyze another binding pocket, at the RNA binding site of SNRNP200, targeted by another inhibitor (PDB code 5URM). I superimposed the ligand-bound structure of the human helicase (PDB ID 5URM) onto SARS-CoV-2 NSP13 (PDB ID 7RDY) to determine if this ligand is suitable for repurposing.
Again, I find that this inhibitor is unlikely to bind to SARS-CoV-2 because the residues the inhibitor interacts with are not conserved. However, even though it is not conserved, a druggable binding pocket is present at the same location and may be used as a potential target for the development of future antivirals.
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