Figure 4.
Figure 4. Impact of YO compounds on Plg conformation. (Top panel) SAXS experiment shows that YO inhibitors do not have an impact on the conformation of full-length Plg. In the presence of TXA (1 mM), Plg switches from the closed (Plg) to the open conformation (Plg + TXA), as reflected by the change in the scattering profile (shape of the curve; supplemental Figure 2). The profile of Plg remains unaltered after incubating with YO inhibitors (Plg + YO-2 and Plg + PSI-112) as detailed in supplemental Data, suggesting that the YO inhibitors cannot trigger conformational change of Plg and therefore, they do not interact with the LBS of KR domains. The SAXS profiles shown are the average of >15 individual images. (Bottom panel) Shown are the radius of gyration (Rg) and maximum dimension of Plg in solution (Dmax) derived from the experiment (see supplemental Data and supplemental Figure 2 for details). Both Rg and Dmax of closed and open Plg are significantly different (P < .0001).

Impact of YO compounds on Plg conformation. (Top panel) SAXS experiment shows that YO inhibitors do not have an impact on the conformation of full-length Plg. In the presence of TXA (1 mM), Plg switches from the closed (Plg) to the open conformation (Plg + TXA), as reflected by the change in the scattering profile (shape of the curve; supplemental Figure 2). The profile of Plg remains unaltered after incubating with YO inhibitors (Plg + YO-2 and Plg + PSI-112) as detailed in supplemental Data, suggesting that the YO inhibitors cannot trigger conformational change of Plg and therefore, they do not interact with the LBS of KR domains. The SAXS profiles shown are the average of >15 individual images. (Bottom panel) Shown are the radius of gyration (Rg) and maximum dimension of Plg in solution (Dmax) derived from the experiment (see supplemental Data and supplemental Figure 2 for details). Both Rg and Dmax of closed and open Plg are significantly different (P < .0001).

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