Dissecting an allosteric switch in caspase-7 using chemical and mutational probes.

@article{Hardy2009DissectingAA,
  title={Dissecting an allosteric switch in caspase-7 using chemical and mutational probes.},
  author={Jeanne A Hardy and James A. Wells},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 38},
  pages={26063-9}
}
Apoptotic caspases, such as caspase-7, are stored as inactive protease zymogens, and when activated, lead to a fate-determining switch to induce cell death. We previously discovered small molecule thiol-containing inhibitors that when tethered revealed an allosteric site and trapped a conformation similar to the zymogen form of the enzyme. We noted three structural transitions that the compounds induced: (i) breaking of an interaction between Tyr-223 and Arg-187 in the allosteric site, which… CONTINUE READING

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