首页|Solution structure of c-FLIP death effector domains
Solution structure of c-FLIP death effector domains
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NSTL
The formation of death-inducing signaling complex (DISC) and death effector domain (DED) filament initiates extrinsic apoptosis。 Recruitment and activation of procaspase-8 at the DISC are regulated by c-FLIP。 The interaction between c-FLIP and procaspase-8 is mediated by their tandem DEDs (tDED)。 However， the structure of c-FLIPtDED and how c-FLIP interferes with procaspase-8 activation at the DISC remain elusive。 Here， we solved the monomeric structure of c-FLIPtDED (F114G) at near physiological pH by solution nuclear magnetic resonance (NMR)。 Structural superimposition reveals c-FLIPtDED (F114G) adopts a structural topology similar to that of procaspase-8tDED。 Our results provide a structural basis for understanding how c-FLIP interacts with procaspase-8 and the molecular mechanisms of c-FLIP in regulating cell death。
Anti-apoptosisc-FLIPDeath effector domains
Zhi-Qiang Bai、Xiaofang Ma、Bin Liu、Tao Huang、Kaifeng Hu
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State Key Laboratory of Phytochemistry and Plant Resources in West China, Kunming Institute of
2022
Biochemical and Biophysical Research Communications
NSTL
