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Crystal structure of the death effector domains of caspase-8.

Shen C, Yue H, Pei J, Guo X, Wang T, Quan JM
Biochem Biophys Res Commun 463 297-302 (2015)
Cited: 18 times
EuropePMC logo PMID: 26003730

Abstract

Caspase-8 is a key mediator in various biological processes such as apoptosis, necroptosis, inflammation, T/B cells activation, and cell motility. Caspase-8 is characterized by the N-terminal tandem death effector domains (DEDs) and the C-terminal catalytic protease domain. The DEDs mediate diverse functions of caspase-8 through homotypic interactions of the DEDs between caspase-8 and its partner proteins. Here, we report the first crystal structure of the DEDs of caspase-8. The overall structure of the DEDs of caspase-8 is similar to that of the DEDs of vFLIP MC159, which is composed of two tandem death effector domains that closely associate with each other in a head-to-tail manner. Structural analysis reveals distinct differences in the region connecting helices α2b and α4b in the second DED of the DEDs between caspase-8 and MC159, in which the helix α3b in MC159 is replaced by a loop in caspase-8. Moreover, the different amino acids in this region might confer the distinct features of solubility and aggregation for the DEDs of caspase-8 and MC159.

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  3. The Inflammasome Adaptor ASC Induces Procaspase-8 Death Effector Domain Filaments. Vajjhala PR, Lu A, Brown DL, Pang SW, Sagulenko V, Sester DP, Cridland SO, Hill JM, Schroder K, Stow JL, Wu H, Stacey KJ. J Biol Chem 290 29217-29230 (2015)
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