6M6O
NMR SOLUTION STRUCTURE OF A C-FLIPs
Summary for 6M6O
Entry DOI | 10.2210/pdb6m6o/pdb |
Descriptor | CASP8 and FADD-like apoptosis regulator (1 entity in total) |
Functional Keywords | apoptosis, c-flips |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 1 |
Total formula weight | 21588.22 |
Authors | |
Primary citation | Bai, 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: 35688044DOI: 10.1016/j.bbrc.2022.05.086 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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