Fas-associated Death Domain protein-protein interaction domain
Death domain (DD) found in FAS-associated via death domain (FADD). FADD is a component of the death-inducing signaling complex (DISC) and serves as an adaptor in the signaling pathway of death receptor proteins. It modulates apoptosis as well as non-apoptotic processes such as cell cycle progression, survival, innate immune signaling, and hematopoiesis. FADD contains an N-terminal DED and a C-terminal DD. Its DD interacts with the DD of the activated death receptor, FAS, and its DED recruits the initiator caspases, caspase-8 and -10, to the DISC complex via a homotypic interaction with the N-terminal DED of the caspase. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes.
Structure:3EZQB: Human FADD death domain interacts with the FAS death domain, contacts at 4A - View structure with Cn3D
Comment:The FAS-FADD death domain complex is an octamer, containing four FAS and four FADD DDs, arranged as a dimer of tetramers, with the tetramer containing two FAS-FADD heterodimers.
Jiyao W et al.(2023). "The conserved domain database in 2023.",