Fig. 6: Mechanisms that prescribe the intrinsically higher catalytic activity of mcGAS vs. hcGAS.
From: The structural basis for 2′−5′/3′−5′-cGAMP synthesis by cGAS
A The binding affinities of mcGAScat and full-length mcGAS(FL) toward various lengths of FAM-labeled dsDNA were determined by tracking the changes in fluorescence anisotropy (FA). B The catalytic activity of mcGAS and hcGAS. C Catalytic activity of mcGAScat vs. WT- and “mouseneized”-hcGAScat toward various NTPs. p values from left to right: **p = 0.0024; ***p = 0.0007; **p = 0.001; ***p = 0.0003; ***p = 0.0001; ***p = 0.0003. D An overlay of ATP/GTP-bound or pppGpA-bound mcGAScat•dsDNA (7uxw and 7v0w) vs. ATP-bound hcGAScat•dsDNA (6cta). E WT- and “mousenized”-hcGAScat•dsDNA reaction products resulting from ATP/GTP were resolved by HPLC (1 hr reaction time, 27 min gradient). F IFN-luc reporter activities from HEK293T cells upon co-transfecting STING and indicated cGAS variants. p values from left to right: **p = 0.006; **p = 0.005.
