Death domain of FAS or TNF receptor superfamily member 6
Death Domain (DD) found in the FS7-associated cell surface antigen (FAS). FAS, also known as TNFRSF6 (TNF receptor superfamily member 6), APT1, CD95, FAS1, or APO-1, together with FADD (Fas-associating via Death Domain) and caspase 8, is an integral part of the death inducing signalling complex (DISC), which plays an important role in the induction of apoptosis and is activated by binding of the ligand FasL to FAS. FAS also plays a critical role in self-tolerance by eliminating cell types (autoreactive T and B cells) that contribute to autoimmunity. 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 can recruit other proteins into signaling complexes.
Structure:3EZQ_A: Human FAS death domain interacts with FADD death domain, contacts at 4A
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.",