4ZBW

Crystal structure of death effector domain of Caspase8 in Homo Sapiens

Summary for 4ZBW

• Entry DOI: 10.2210/pdb4zbw/pdb
• Descriptor: Caspase-8 (2 entities in total)
• Functional Keywords: death effector domain, caspase, hydrolase
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm: Q14790
• Total number of polymer chains: 2
• Total formula weight: 44977.76

Authors

Shen, C.,Wang, T.,Quan, J. (deposition date: 2015-04-15, release date: 2015-07-01, Last modification date: 2023-11-08)

Primary citation

Shen, C.,Yue, H.,Pei, J.,Guo, X.,Wang, T.,Quan, J.M.
Crystal structure of the death effector domains of caspase-8
Biochem.Biophys.Res.Commun., 463:297-302, 2015

PubMed 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.

PubMed: 26003730
DOI: 10.1016/j.bbrc.2015.05.054

Experimental method

X-RAY DIFFRACTION (2.2 Å)