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Evolution of an allosteric "off switch" in apoptotic caspases.


ABSTRACT: Caspase-3 is well known as the "executioner" whose activation commits the cell to an apoptotic fate, but low levels of caspase-3 activity also play key roles in development. A new study explains how cells can balance these functions, using biophysical, structural, and computational approaches to demonstrate the mechanism by which phosphorylation of conserved sites on a distal surface loop reduces or abolishes catalytic activity. These results provide new insights into allosteric regulation mechanisms and offer new opportunities for development of caspase-3 modulators.

SUBMITTER: Herr AB 

PROVIDER: S-EPMC5900751 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature

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Evolution of an allosteric "off switch" in apoptotic caspases.

Herr Andrew B AB  

The Journal of biological chemistry 20180401 15


Caspase-3 is well known as the "executioner" whose activation commits the cell to an apoptotic fate, but low levels of caspase-3 activity also play key roles in development. A new study explains how cells can balance these functions, using biophysical, structural, and computational approaches to demonstrate the mechanism by which phosphorylation of conserved sites on a distal surface loop reduces or abolishes catalytic activity. These results provide new insights into allosteric regulation mecha  ...[more]

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2014-12-03 | GSE63794 | GEO