| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1979203 | Current Opinion in Structural Biology | 2012 | 7 Pages |
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.
► Death domain oligomerization is facilitated by conserved interaction surfaces. ► Known death domain oligomers possess helical symmetry. ► Helical oligomerization provides a versatile digital signal propagation mechanism.
