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Curr Opin Struct Biol. 2012 Apr;22(2):241-7. doi: 10.1016/j.sbi.2012.02.006. Epub 2012 Mar 17.

Helical assembly in the death domain (DD) superfamily.

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1
Department of Biochemistry, Weill Cornell Medical College and Graduate School of Medical Sciences, New York, NY 10021, USA.

Abstract

Death domain (DD) superfamily members play a central role in apoptotic and inflammatory signaling through formation of oligomeric molecular scaffolds. These scaffolds promote the activation of proinflammatory and apoptotic initiator caspases, as well as Ser/Thr kinases. Interactions between DDs are facilitated by a conserved set of interaction surfaces, type I, type II, and type III. Recently structural information on a ternary complex containing the DDs of MyD88, IRAK4, and IRAK2 and a binary complex containing Fas and FADD DDs has become available. This review will focus on how the three DD interaction surfaces cooperate to facilitate the assembly of these oligomeric signaling complexes.

PMID:
22429337
PMCID:
PMC3320699
DOI:
10.1016/j.sbi.2012.02.006
[Indexed for MEDLINE]
Free PMC Article
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