Literature summary for 3.4.22.61 extracted from

Park, H.H.
Molecular basis of dimerization of initiator caspase was revealed by crystal structure of caspase-8 pro-domain (2019), Cell Death Differ., 26, 1213-1220 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of caspase-8 tandem death effector domains (DEDs), reveals domain-swapped dimerization. DEDs exist as dimers in solution. The FL motif on DED2 is critical for caspase-8 dimerization via domain swapping	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q14790	-	-

General Information

General Information	Comment	Organism
metabolism	model of caspase 8 activation. Upon apoptosis induction triggered by interaction of the death ligand to the trimeric death receptor, adaptor FADD (Fas-associated protein with death domain ) is recruited to the death receptor via a death domain DD-DD interaction. FADD recruited at cell surface can recruit caspase-8 via a DED-DED interaction, leading to procaspase-8 proximity to meet another procaspase-8. Closely located FL motif on DED2 causes domain swapping and dimerization of procaspase-8. The dimerization via tandem DED domain swapping causes the proximity-mediated self-activation of caspase-8	Homo sapiens

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Release 2023.1 (January 2023)