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The death domain superfamily in intracellular signaling of apoptosis and inflammation

Authors
Park, Hyun HoLo, Yu-ChihLin, Su-ChangWang, LiweiYang, Jin KukWu, Hao
Issue Date
Apr-2007
Publisher
ANNUAL REVIEWS
Keywords
death domain (DD); death effector domain (DED); tandem DED; caspase recruitment domain (CARD); pyrin domain (PYD); crystal structure; NMR structure
Citation
ANNUAL REVIEW OF IMMUNOLOGY, v.25, pp.561 - 586
Journal Title
ANNUAL REVIEW OF IMMUNOLOGY
Volume
25
Start Page
561
End Page
586
URI
http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/31343
DOI
10.1146/annurev.immunol.25.022106.141656
ISSN
0732-0582
Abstract
The death domain (DD) superfamily comprising the death domain (DD) subfamily, the death effector domain (DED) subfamily, the caspase recruitment domain (CARD) subfamily, and the pyrin domain (PYD) subfamily is one of the largest domain superfamilies. By mediating homotypic interactions within each domain subfamily, these proteins play important roles in the assembly and activation of apoptotic and inflammatory complexes. In this chapter, we review the molecular complexes assembled by these proteins, the structural and biochemical features of these domains, and the molecular interactions mediated by diem. By analyzing the potential molecular basis for the function of these domains, we hope to provide a comprehensive understanding of the function, structure, interaction, and evolution of this important family of domains.
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