Death effector domain

Death effector domain
structure of the FADD (Mort1) death-effector domain.[1]
Identifiers
Symbol	DED
Pfam	PF01335
InterPro	IPR001875
SMART	DED
PROSITE	PS50168
SCOP2	1a1z / SCOPe / SUPFAM
CDD	cd00045
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary PDB 1a1w​, 1a1z​, 1e3y​, 1e41​, 1n3k​, 2gf5​

The death-effector domain (DED) is a protein interaction domain found only in eukaryotes that regulates a variety of cellular signalling pathways.^[2] The DED domain is found in inactive procaspases (cysteine proteases) and proteins that regulate caspase activation in the apoptosis cascade such as FAS-associating death domain-containing protein (FADD). FADD recruits procaspase 8 and procaspase 10 into a death induced signaling complex (DISC). This recruitment is mediated by a homotypic interaction between the procaspase DED and a second DED that is death effector domain in an adaptor protein that is directly associated with activated TNF receptors. Complex formation allows proteolytic activation of procaspase into the active caspase form which results in the initiation of apoptosis (cell death). Structurally the DED domain are a subclass of protein motif known as the death fold and contains 6 alpha helices, that closely resemble the structure of the Death domain (DD).