首页|Solution structure of c-FLIP death effector domains
Solution structure of c-FLIP death effector domains
扫码查看
点击上方二维码区域，可以放大扫码查看
原文链接
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
展开 >
State Key Laboratory of Phytochemistry and Plant Resources in West China, Kunming Institute of
2022
Biochemical and Biophysical Research Communications
NSTL
