Cryo-EM structural analysis of FADD:Caspase-8 complexes defines the catalytic dimer architecture for co-ordinated control of cell fate

Cryo-EM structural analysis of FADD:Caspase-8 complexes defines the catalytic dimer architecture for co-ordinated control of cell fate

The core FADD:Caspase-8 complex and its regulatory partners, such as the cell death inhibitor c-FLIP, coordinate cell fate. Here authors present the structure of full-length procaspase-8 in a complex with FADD and reveal how recruitment of c-FLIPS into this complex inhibits Caspase-8 activity.

Bibliographic Details
Main Authors: Joanna L. Fox, Michelle A. Hughes, Xin Meng, Nikola A. Sarnowska, Ian R. Powley, Rebekah Jukes-Jones, David Dinsdale, Timothy J. Ragan, Louise Fairall, John W. R. Schwabe, Nobuhiro Morone, Kelvin Cain, Marion MacFarlane
Format: Article
Language:English
Published: Nature Portfolio 2021-02-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-020-20806-9

Internet

https://doi.org/10.1038/s41467-020-20806-9

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