Substrate and inhibitor-induced dimerization and cooperativity in caspase-1 but not caspase-3.

@article{Datta2013SubstrateAI,
  title={Substrate and inhibitor-induced dimerization and cooperativity in caspase-1 but not caspase-3.},
  author={Debajyoti Datta and Christopher L. McClendon and Matthew P. Jacobson and James A. Wells},
  journal={The Journal of biological chemistry},
  year={2013},
  volume={288 14},
  pages={
          9971-81
        }
}
Caspases are intracellular cysteine-class proteases with aspartate specificity that is critical for driving processes as diverse as the innate immune response and apoptosis, exemplified by caspase-1 and caspase-3, respectively. Interestingly, caspase-1 cleaves far fewer cellular substrates than caspase-3 and also shows strong positive cooperativity between the two active sites of the homodimer, unlike caspase-3. Biophysical and kinetic studies here present a molecular basis for this difference… CONTINUE READING

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