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
SCOP	1a1z
CDD	cd00045
Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary

The death-effector domain (DED) is a protein interaction domain found to regulate 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.

References

1. ^ Eberstadt M, Huang B, Chen Z, et al. (April 1998). "NMR structure and mutagenesis of the FADD (Mort1) death-effector domain". Nature 392 (6679): 941–5. doi:10.1038/31972. PMID 9582077. 
2. ^ Valmiki MG, Ramos JW (March 2009). "Death effector domain-containing proteins". Cell. Mol. Life Sci. 66 (5): 814–30. doi:10.1007/s00018-008-8489-0. PMID 18989622. 

External links

• The Nash Lab: DED

This protein-related article is a stub. You can help Wikipedia by expanding it.v · Categories: Protein stubs Protein domains Wikimedia Foundation. 2010. Игры ⚽ Поможем написать реферат Chiarano Mäxmüd of Kazan Look at other dictionaries: death-effector domain — Domain at the C terminus of FADD and N terminus of FLICE. Interaction mediated by these domains leads to the assembly of the death inducing signalling complex (DISC) which activates other caspases …   Dictionary of molecular biology Death domain — Structure of the Fas (APO 1/CD95) death domain.[1] Identifiers Symbol Death …   Wikipedia Death fold — Cartoon representation of the molecular structure of a death domain protein. 1ngr The death fold is a tertiary structure motif commonly found in proteins involved in apoptosis or inflammation related processes. This motif is com …   Wikipedia CARD domain — Caspase recruitment domains, or CARD domains, are interaction motifs found in a wide array of proteins, typically those involved in processes relating to inflammation and apoptosis. These domains mediate the formation of larger protein complexes… …   Wikipedia Protein domain — Pyruvate kinase, a protein from three domains (PDB 1pkn) A protein domain is a part of protein sequence and structure that can evolve, function, and exist independently of the rest of the protein chain. Each domain forms a compact three… …   Wikipedia DEDD — Death effector domain containing Identifiers Symbols DEDD; CASP8IP1; DEDD1; DEFT; FLDED1 External IDs …   Wikipedia DISC — (= death inducing signalling complex) See death effector domain …   Dictionary of molecular biology Caspase — Caspases, or c ysteine asp artic acid prote ases , are a family of cysteine proteases, which play essential roles in apoptosis (programmed cell death), necrosis and inflammation. Caspases are essential in cells for apoptosis, one of the main… …   Wikipedia Fas receptor — The Fas receptor (FasR) is the most intensely studied death receptor. Its aliases include CD95, Apo 1, and tumor necrosis factor receptor superfamily, member 6 (TNFRSf6). The gene is situated on chromosome 10 in humans and 19 in mice.… …   Wikipedia Fas ligand — (FasL) is a type II transmembrane protein that belongs to the tumor necrosis factor (TNF) family. The binding of Fas ligand with its receptor induces apoptosis. Fas ligand receptor interactions play an important role in the regulation of the… …   Wikipedia 18+ © Academic, 2000-2024 Contact us: Technical Support, Advertising Dictionaries export, created on PHP, Joomla, Drupal, WordPress, MODx. Mark and share Search through all dictionaries Translate… Search Internet Share the article and excerpts Direct link … Do a right-click on the link above and select “Copy Link”