Department of Biochemistry, Weill Cornell Medical College and Graduate School of Medical Sciences, New York, NY 10021, USA.
Curr Opin Struct Biol. 2012 Apr;22(2):241-7. doi: 10.1016/j.sbi.2012.02.006. Epub 2012 Mar 17.
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.
死亡结构域（DD）超家族成员通过形成寡聚分子支架，在凋亡和炎症信号中发挥核心作用。这些支架促进炎症和凋亡起始半胱氨酸蛋白酶的激活，以及 Ser/Thr 激酶的激活。DD 之间的相互作用是通过一组保守的相互作用表面，即 I 型、II 型和 III 型来促进的。最近，含有 MyD88、IRAK4 和 IRAK2 的 DD 的三元复合物以及含有 Fas 和 FADD DD 的二元复合物的结构信息已经可用。这篇综述将重点介绍这三个 DD 相互作用表面如何协同作用，促进这些寡聚信号复合物的组装。
