Death effector domain
Encyclopedia
The death-effector domain (DED) is a protein interaction domain found to regulate a variety of cellular signalling pathways. The DED domain is found in inactive procaspases (cysteine protease
s) 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
.
Cysteine protease
Proteases are enzymes that degrade polypeptides. Cysteine proteases have a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic dyad. The first step is deprotonation of a thiol in the enzyme's active site by an adjacent amino acid with a basic side chain, usually a...
s) and proteins that regulate caspase activation in the apoptosis cascade such as FAS-associating death domain-containing protein (FADD
FADD
Fas-Associated protein with Death Domain is an adaptor molecule that bridges the Fas-receptor, and other death receptors, to caspase-8 through its death domain to form the death-inducing signaling complex during apoptosis. -Signalling:...
). 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
Adaptor protein
Signal transducing adaptor proteins are proteins which are accessory to main proteins in a signal transduction pathway. These proteins tend to lack any intrinsic enzymatic activity themselves but instead mediate specific protein–protein interactions that drive the formation of protein complexes...
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
Apoptosis
Apoptosis is the process of programmed cell death that may occur in multicellular organisms. Biochemical events lead to characteristic cell changes and death. These changes include blebbing, cell shrinkage, nuclear fragmentation, chromatin condensation, and chromosomal DNA fragmentation...
(cell death). Structurally the DED domain are a subclass of protein motif known as the death fold
Death fold
The death fold is a tertiary structure motif commonly found in proteins involved in apoptosis or inflammation-related processes. This motif is commonly found in domains that participate in protein-protein interactions leading to the formation of large functional complexes...
and contains 6 alpha helices, that closely resemble the structure of the Death domain
Death domain
The death domain is a protein interaction module composed of a bundle of six alpha-helices. DD is a subclass of protein motif known as the death fold and is related in sequence and structure to the death effector domain and the caspase recruitment domain , which work in similar pathways and show...
.