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Caspase activation, inhibition, and reactivation: a mechanistic view Shi YProtein Sci 2004[Aug]; 13 (8): 1979-87Caspases, a unique family of cysteine proteases, execute programmed cell death (apoptosis). Caspases exist as inactive zymogens in cells and undergo a cascade of catalytic activation at the onset of apoptosis. The activated caspases are subject to inhibition by the inhibitor-of-apoptosis (IAP) family of proteins. This inhibition can be effectively removed by diverse proteins that share an IAP-binding tetrapeptide motif. Recent structural and biochemical studies have revealed the underlying molecular mechanisms for these processes in mammals and in Drosophila. This paper reviews these latest advances.|Amino Acid Motifs[MESH]|Animals[MESH]|Apoptosis/*physiology[MESH]|Caspases/*chemistry/*metabolism[MESH]|Drosophila/metabolism[MESH]|Enzyme Activation/physiology[MESH]|Enzyme Reactivators/metabolism[MESH]|Humans[MESH]|Inhibitor of Apoptosis Proteins[MESH]|Mammals/metabolism[MESH]|Protein Structure, Tertiary[MESH]|Proteins/*chemistry/*metabolism[MESH] |
