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The death-effector domain (DED) is a protein interaction domain found only in eukaryotes that regulates a variety of cellular signalling pathways. 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

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rdf:type
rdfs:label
  • Death effector domain (en)
rdfs:comment
  • The death-effector domain (DED) is a protein interaction domain found only in eukaryotes that regulates a variety of cellular signalling pathways. 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 (en)
name
  • Death effector domain (en)
foaf:depiction
  • http://commons.wikimedia.org/wiki/Special:FilePath/Active_non-apoptotic_protease.png
  • http://commons.wikimedia.org/wiki/Special:FilePath/Molecular_assembly_of_FADD_forming_DED_chain-like_structure.png
  • http://commons.wikimedia.org/wiki/Special:FilePath/PDB_1a1z_EBI.jpg
  • http://commons.wikimedia.org/wiki/Special:FilePath/Processing_of_procaspase-8.png
  • http://commons.wikimedia.org/wiki/Special:FilePath/Ribbondiagram_of_DED.jpg
dct:subject
Wikipage page ID
Wikipage revision ID
Link from a Wikipage to another Wikipage
Link from a Wikipage to an external page
sameAs
dbp:wikiPageUsesTemplate
thumbnail
PROSITE
  • PS50168 (en)
SCOP
SMART
  • DED (en)
bot
  • InternetArchiveBot (en)
caption
  • structure of the FADD death-effector domain. (en)
date
  • July 2019 (en)
fix-attempted
  • yes (en)
InterPro
  • IPR001875 (en)
Pfam
  • PF01335 (en)
symbol
  • DED (en)
has abstract
  • The death-effector domain (DED) is a protein interaction domain found only in eukaryotes that regulates a variety of cellular signalling pathways. 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). (en)
CDD
  • cd00045 (en)
PDB
  • , , , , , (en)
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