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6M6O

NMR SOLUTION STRUCTURE OF A C-FLIPs

Summary for 6M6O
Entry DOI10.2210/pdb6m6o/pdb
DescriptorCASP8 and FADD-like apoptosis regulator (1 entity in total)
Functional Keywordsapoptosis, c-flips
Biological sourceHomo sapiens (Human)
Total number of polymer chains1
Total formula weight21588.22
Authors
Bai, Z.Q.,Hu, K.F. (deposition date: 2020-03-16, release date: 2021-03-17, Last modification date: 2024-05-15)
Primary citationBai, Z.Q.,Ma, X.,Liu, B.,Huang, T.,Hu, K.
Solution structure of c-FLIP death effector domains.
Biochem.Biophys.Res.Commun., 617:1-6, 2022
Cited by
PubMed Abstract: 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-FLIP and how c-FLIP interferes with procaspase-8 activation at the DISC remain elusive. Here, we solved the monomeric structure of c-FLIP (F114G) at near physiological pH by solution nuclear magnetic resonance (NMR). Structural superimposition reveals c-FLIP (F114G) adopts a structural topology similar to that of procaspase-8. 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.
PubMed: 35688044
DOI: 10.1016/j.bbrc.2022.05.086
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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