User:Christopher French
CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-8 WITH THE TETRAPEPTIDE INHIBITOR ACE-IETD-ALDEHYDECRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-8 WITH THE TETRAPEPTIDE INHIBITOR ACE-IETD-ALDEHYDE
Caspase 8 is a member of the caspase family, a family of cysteine proteases that play an important role in inflammation and apoptosis or programmed cell death. The caspases are essential for apoptosis in cells during development and during later stages of life. Failure of apoptosis can lead to tumor formation and the development of autoimmune diseases. In addition, excess apoptosis has been implicated in various disease states, including ischemia and Alzheimer’s. Caspase 8 is just one of 11 caspases that have been indentified in humans. Caspase 8 is an “initiator caspase” which cleave inactive pro-forms of the effectors caspases and subsequently activating them. Caspases exist as inactive proenzymes that are composed of a prodomain, and a large and small protease subunit. The activation of caspase requires proteolysis at an internal aspartic residue which results in the generation of a heterodimeric enzyme with a large and small subunit. File:Apoptosiscascade.jpg
Caspase 8 is induced by tumor necrosis (TNF)-related apoptosis-inducing ligand (TRAIL). TRAIL induces apoptosis via death receptors (DR4 and DR5). After ligand binding the death receptor Fas recruits the adaptor protein FADD. FADD then binds and activates procaspase-8. Upon activation, Caspase 8 is then able activate caspase 3 and other downstream effectors. The end result is apoptosis. File:Caspase8cascade.gif
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