Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition

Article Abstract:

Smac is a mitochondrial protein that eliminates IAP inhibition, thereby promoting cytochrome c-dependent caspase activation. Identification of this novel protein is reported. Overexpressed Smac increases sensitivity of cells. It is the second mitochondrial protein, with cytochrome c, that brings on apoptosis by activating caspases. Mitochondrial import and cleavage of its signal peptide are needed for Smac to get its apoptotic activity.

Research, Carrier proteins, Transport proteins, Cytochemistry

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Structure of Bax: coregulation of dimer formation and intracellular localization

Article Abstract:

Research describes the solution structure of Bax protein involved in the programmed cell death via mitochondrial targeting and dimer formation. Data reveal that Bax protein consists of 9 alpha helices and apoptosis is initiated by insertion of the protein from cytoplasm into mitochondrial memebranes through helix alpha9.

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Crystal structure of a procaspase-7 zymogen: mechanisms of activation and substrate binding

Article Abstract:

The crystal structures of an unprocessed procaspase-7 zymogen and an active caspase-7 reveal large conformational changes resulting from interdomain cleavage and bound inhibitor. Data show structural differences surrounding the catalytic cleft of procaspase-7 zymogen and proteolytic cleavage between subunits, which leads to changes in the active site and inhibitor/substrate binding.

Statistical Data Included, Analysis, Structure-activity relationships (Biochemistry)

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