Fig. 6: G243-1720 stabilizes the sOPG57 dimer.

A Analytical ultracentrifugation of sOPG057 in the absence (gray line) or presence of 10 μM tecovirimat (yellow line) or 10 μM G243-1720 (green line). Experimentally derived sedimentation coefficient values (Svedberg units (S)) are indicated above each peak. c(s) is the concentration of protein with sedimentation coefficient s. B Mass-photometry assay used to estimate the dimerization activity of G243-1720 in solution using sOPG057^WT and G243-1720 escape mutants. The y-axis represents the proportion of sOPG057 dimer, the different columns represent the dimerization degree of sOPG057^WT or different OPG057 mutants in the absence or presence of 10 μM G243-1720 or tecovirimat. Data are mean ± s.d. of three independent experiments (n = 3). C Experimental SAXS profile (green dots) and theoretical profiles (dashed lines) for one monomer of sOPG057 (blue dashed line) and the dimer (pink dashed line) are shown. I(q), scattering intensity as a function of the scattering vector q; q(Å^-1), scattering vector; Å, Angstrom; X², chi-squared test. D Orthogonal views of a representative dummy atom model (green) reconstructed from SAXS data. For comparison, we included below a model of the crystallographic sOPG057 dimer with an outline of the dummy model. Data in (B) are from three independent experiments, and each was performed in triplicate. Statistical significance was determined by unpaired, two-tailed Student’s t-test (n = 3; mean ± s.d.; ns, not significant; ****P < 0.0001). Source data are provided as a Source Data file.