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.

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Detalles Bibliográficos
Autores principales: 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
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
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Science
Q
Acceso en línea:https://doaj.org/article/cbf43a167d5c47dbbf9efdc46a691fd7
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Sumario: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.

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