Knowledge of the molecular mechanisms of activation of Clostridium difficile toxins will significantly enhance the ability to design specific anti-virulence therapies. Using activity-based chemical probes in combination with other techniques, this study reveals mechanistic insights into how inositol hexakisphosphate binding at the active site of the cysteine protease domain shifts the conformational equilibrium towards an active conformer.
- Aimee Shen
- Patrick J Lupardus
- Matthew Bogyo
