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- W2116764248 abstract "Apaf-1 and cytochrome c coassemble in the presence of dATP to form the apoptosome. We have determined a structure of the apoptosome at 12.8 A resolution by using electron cryomicroscopy and single-particle methods. We then docked appropriate crystal structures into the map to create an accurate domain model. Thus, we found that seven caspase recruitment domains (CARDs) form a central ring within the apoptosome. At a larger radius, seven copies of the nucleotide binding and oligomerization domain (NOD) associate laterally to form the hub, which encircles the CARD ring. Finally, an arm-like helical domain (HD2) links each NOD to a pair of beta propellers, which bind a single cytochrome c. This model provides insights into the roles of dATP and cytochrome c in assembly. Our structure also reveals how a CARD ring and the central hub combine to create a platform for procaspase-9 activation." @default.
- W2116764248 created "2016-06-24" @default.
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- W2116764248 date "2005-11-01" @default.
- W2116764248 modified "2023-10-13" @default.
- W2116764248 title "A Structure of the Human Apoptosome at 12.8 Å Resolution Provides Insights into This Cell Death Platform" @default.
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- W2116764248 doi "https://doi.org/10.1016/j.str.2005.09.006" @default.
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