Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 463, Issue 3, Pages 297-302Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2015.05.054
Keywords
Caspase-8; Death effector domain; Apoptosis; Necroptosis; Inflammation
Categories
Funding
- Ministry of Science and Technology [2012CB722602, 2013CB911501]
- NSFC [21290183, 81373326, NSFC31300600]
- Shenzhen government [JCYJ20130331144947526, GJHZ20120614144733420, KQCX20130627103353535, GGJS20130329180714793]
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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 hornotypic 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 alpha 2b and alpha 4b in the second DED of the DEDs between caspase-8 and MC159, in which the helix alpha 3b 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. (C) 2015 Elsevier Inc. All rights reserved.
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