Fig. 3: Disruption of the S284/A285/L286 dimerization interface in the disulfide-containing structure.
From: SARS-CoV-2 Mpro responds to oxidation by forming disulfide and NOS/SONOS bonds
Shown is the region where the loop containing S284, A285, and L286 forms a hydrophobic zipper with the same residues on the opposite dimer-forming protomer. All four structures reported are drawn, A reduced/C2 (orange, PDB ID: 7PXZ), reduced/P212121 (yellow, PDB ID: 7Z2K), NOS/SONOS (purple, PDB ID: 7Z3U), and B C117-C145 (teal, PDB ID: 7PZQ). Only the C117-C145 structure shows a disruption of this dimer interface. For these three residues, the buried surface area decreases from ~110 Å2 for the structures in A to 87 and 85 Å2 for molecules A and B of the C117-C145 structure shown in B, respectively. Structures were aligned by minimizing all heavy atom RMSD prior to visualization. Surfaces are the solvent-accessible (Connolly) surface computed with the PyMOL Molecular Graphics System (2.0, Schrödinger LLC)48.
