Jad Walters

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The caspase-3 zymogen has essentially zero activity until it is cleaved by initiator caspases during apoptosis. However, a mutation of V266E in the dimer interface activates the protease in the absence of chain cleavage. We show that low concentrations of the pseudo-activated procaspase-3 kill mammalian cells rapidly and, importantly, this protein is not(More)
A mutation in the allosteric site of the caspase 3 dimer interface of Val266 to histidine abolishes activity of the enzyme, and models predict that the mutation mimics the action of small molecule allosteric inhibitors by preventing formation of the active site. Mutations were coupled to His266 at two sites in the interface, E124A and Y197C. We present(More)
The interface mutants do not affect oligomerization Although the V266E mutation does not change the oligomeric properties of caspase-3 at higher protein concentrations (micromolar range) [1], we examined whether the mutation weakens the dimer interface at lower protein concentrations by performing dilution experiments coupled with enzyme activity(More)
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