Helical assembly in the death domain (DD) superfamily

被引：117

作者：

Ferrao, Ryan

Wu, Hao ^{[1
]}

机构：

[1] Weill Cornell Med Coll, Dept Biochem, New York, NY 10021 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2012年 / 22卷 / 02期

关键词：

NF-KAPPA-B; CRYSTAL-STRUCTURE; PYRIN DOMAIN; NMR STRUCTURE; DIGITAL ACTIVATION; SIGNALING PLATFORM; EFFECTOR DOMAIN; COMPLEX; RECEPTOR; FADD;

D O I：

10.1016/j.sbi.2012.02.006

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

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页码：241 / 247

页数：7

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