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• W2057604385 abstract "Apaf-1 coassembles with cytochrome c to form the apoptosome, which then binds and activates procaspase-9 (pc-9). We removed pc-9 catalytic domains from the holoapoptosome by site-directed thrombinolysis. A structure of the resulting apoptosome-pc-9 CARD complex was then determined at ∼9.5 Å resolution. In our model, the central hub is constructed like other AAA+ protein rings but also contains novel features. At higher radius, the regulatory region of each Apaf-1 is comprised of tandem seven and eight blade β-propellers with cytochrome c docked between them. Remarkably, Apaf-1 CARDs are disordered in the ground state. During activation, each Apaf-1 CARD interacts with a pc-9 CARD and these heterodimers form a flexibly tethered “disk” that sits above the central hub. When taken together, the data reveal conformational changes during Apaf-1 assembly that allow pc-9 activation. The model also provides a plausible explanation for the effects of NOD mutations that have been mapped onto the central hub." @default.
• W2057604385 created "2016-06-24" @default.
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• W2057604385 date "2010-05-01" @default.
• W2057604385 modified "2023-09-25" @default.
• W2057604385 title "Structure of an Apoptosome-Procaspase-9 CARD Complex" @default.
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• W2057604385 doi "https://doi.org/10.1016/j.str.2010.04.001" @default.
• W2057604385 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2874686" @default.
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