Literature summary for 3.4.22.61 extracted from

Xu, G.; Cirilli, M.; Huang, Y.; Rich, R.L.; Myszka, D.G.; Wu, H.
Covalent inhibition revealed by the crystal structure of the caspase-8/p35 complex (2001), Nature, 410, 494-497.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystallization of caspase-8 in complex with p35 protein from baculovirus, at 20°C by hanging-drop vapour diffusion	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
p35	p35 protein from baculovirus inhibits in the active site through a covalent thioester linkage to p35. The p35 protein undergoes dramatic conformational changes on cleavage by the caspase. The repositioning of the amino terminus of p35 into the active site of the caspase eliminates solvent accessibility of the catalytic dyad	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

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Release 2023.1 (January 2023)