Journal
BIOPHYSICAL CHEMISTRY
Volume 101, Issue -, Pages 145-153Publisher
ELSEVIER
DOI: 10.1016/S0301-4622(02)00151-5
Keywords
caspases; inhibitor binding; structure comparison; X-ray structure; apoptosis; zymogen activation
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Apoptosis is primarily executed by active caspases, which are derived from the inactive zymogens. Structural and biochemical studies of caspases-1, -3, -7, -8 and -9 have greatly enhanced our understanding of the structure, function, and specificity of the active form of these enzymes. Only recently, the structures of procaspase-7 and biochemical studies of procaspase-9 and -8 have provided insight into the process of procaspase activation. The mechanism of zymogen activation requires limited proteolysis as for many other proteases. In addition, self-activation through oligomerization has been demonstrated for the initiator caspases-8, -9 and -10. These studies provide a structural mechanism for caspase activation, substrate/inhibitor binding, and contribute to the understanding of the biological role of caspases in the processes of apoptosis. (C) 2002 Elsevier Science B.V All rights reserved.
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