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Topic: DED domain


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In the News (Sun 29 Nov 09)

  
  Structural domain - Wikipedia, the free encyclopedia
Within a protein, a structural domain ("domain") is an element of overall structure that is self-stabilizing and often folds independently of the rest of the protein chain.
Domains often are named and singled out because they figure prominently in the biological function of the protein they belong to; for example, the "calcium-binding" domain of calmodulin.
Given the fact that phosphoinositides are sequestered to various cell membranes (due to their long lipophilic tail) the PH domains usually cause localization of the protein in question to one or another cell membrane, which is useful for expediting activation of the protein and continuation of a signaling pathway.
en.wikipedia.org /wiki/Structural_domain   (558 words)

  
 SH3 domain - Wikipedia, the free encyclopedia
The SH3 domain has a characteristic fold which consists of five or six β-strands arranged as two tightly packed anti-parallel β sheets.
The SH3 domain is found in proteins that interact with other proteins and they mediate assembly of specific protein complexes via binding to proline-rich peptides in their respective binding partner.
SH3 domains are often found in functions concerning the cytoskeleton, the ras protein, and the src kinase.
en.wikipedia.org /wiki/SH3_domain   (153 words)

  
 Structural domain: Facts and details from Encyclopedia Topic   (Site not responding. Last check: 2007-10-18)
Domains often are named and singled out because they figure prominently in the biological function of the protein they belong to; for example, EHandler: no quick summary.
In structural biology, shc, or src homology 2 domain-containing, is a structural domain in signal transduction proteins....
An sh3 domain is a protein module, a characteristic peptide sequence....
www.absoluteastronomy.com /encyclopedia/s/st/structural_domain.htm   (1316 words)

  
 Pfam 19.0 : DED   (Site not responding. Last check: 2007-10-18)
DED is related in sequence and structure to the death domain (DD, see) and the caspase recruitment domain (CARD, see), which work in similar pathways and show similar interaction properties PUBMED:11504623.
The dimerisation of DED domains is mediated primarily by electrostatic interactions.
Domains associated with DED include: caspase catalytic domains (in caspase-8, -10), death domains (in FADD), nuclear localisation sequences (in DEDD), transmembrane domains (in Bap31 and Bar), nucleotide-binding domains (in Dap3), coiled-coil domains (in Hip and Hippi), SAM domains (in Bar), and E2-binding RING domains (in Bar) PUBMED:15226512.
pfam.wustl.edu /cgi-bin/getdesc?name=DED   (212 words)

  
 Patent 6,965,023
The death domain is a conserved protein interaction domain, which usually participates in signal transduction pathways governed by members of the TNF family of cytokine receptors, Toll-family receptors, and/or regulation of apoptosis.
Proteins that bind to the invention DDs, DEDS, and NB-ARC domains, generally, are well known in the art as modulating the cellular pathways that effect apoptosis, cell proliferation, cell adhesion, cell stress responses, responses to microbial infection, and B cell immunoglobulin class switching, and NF-κB and JNK are further known to modulate these pathways.
Invention anti-DD, anti-DED or anti-NB-ARC domain antibodies are contemplated for use herein to modulate the activity of the DD, DED or NB-ARC domain polypeptide in living animals, in humans, or in biological tissues or fluids isolated therefrom.
pharmcast.com /Patents100/Yr2005/Nov2005/111505/6965023_Death111505.htm   (13459 words)

  
 Patent 6,965,023
For example, a test DD, DED or NB-ARC polypeptide can be used to produce antibodies, which are then assayed for their ability to bind to an invention DD, DED or NB-ARC comprising SEQ ID NOS:2, 4, 6, 8, 10, 12, 53, 56 or 58.
DNA probes derived from the DD, DED or NB-ARC gene are particularly useful for this purpose.
Nucleic acids encoding proteins with which the DD, DED or NB-ARC domain, or functional fragment thereof, are fused will also encode, for example, glutathione-S-transferase, an antibody, or other proteins or functional fragments thereof which facilitate recovery of the chimera.
www.pharmcast.com /Patents100/Yr2005/Nov2005/111505/6965023_Death111505.htm   (13459 words)

  
 GeneCard for FADD   (Site not responding. Last check: 2007-10-18)
FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis.
A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain.
NMR structure and mutagenesis of the FADD (Mort1) death-effector domain.
bioinfo.cnio.es /cgi-bin/genecards/carddisp?FADD   (662 words)

  
 Death-effector Filaments: Novel Cytoplasmic Structures that Recruit Caspases and Trigger Apoptosis -- Siegel et al. 141 ...
The death domain is a 60-amino acid portion of the
The DED was originally defined by the minimal portion of the FADD molecule capable of inducing apoptosis in a transient transfection
The hatched bars denote DED, and the checkered bars denote the death domain (DD) in FADD homologous to that in death domain-containing receptors.
www.jcb.org /cgi/content/full/141/5/1243   (6230 words)

  
 The Pawson Lab - Home
Modular protein domains that mediate protein-protein interactions are critical elements of this process.
Since the discovery of SH2 domains, the number of different modules has grown into the dozens, many of which we continue to investigate.
Work on the molecular dissection and functional significance of protein-protein interactions, in signal transduction, is a primary focus of the lab.
pawsonlab.mshri.on.ca   (167 words)

  
 Binding of FADD and Caspase-8 to Molluscum Contagiosum Virus MC159 v-FLIP Is Not Sufficient for Its Antiapoptotic ...   (Site not responding. Last check: 2007-10-18)
region that is termed the death domain (13).
The RXDL motif (denoted by bars) is located at amino acids 69 to 72 in DED-A and amino acids 166 to 169 in DED-B. The asterisks indicate the amino acids in hydrophobic patch 1.
A domain in TNF receptors that mediates ligand-independent receptor assembly and signaling.
jvi.asm.org /cgi/content/full/76/2/697   (5343 words)

  
 Pfam 19.0 : Death   (Site not responding. Last check: 2007-10-18)
The death domain (DD) is a homotypic protein interaction module composed of a bundle of six alpha-helices.
DD is related in sequence and structure to the death effector domain (DED, see) and the caspase recruitment domain (CARD, see), which work in similar pathways and show similar interaction properties PUBMED:11504623.
The death domain motif found in Fas (Apo-1) and Tnf receptor is Present in proteins involved in apoptosis and axonal guidance.
pfam.wustl.edu /cgi-bin/getdesc?name=Death   (298 words)

  
 BAR: An apoptosis regulator at the intersection of caspases and Bcl-2 family proteins -- Zhang et al. 97 (6): 2597 -- ...
The presence of a candidate TM domain in BAR suggested it could be a membrane-associated protein.
DED Domain of BAR Is Required for Interactions with Procaspases-8 and -10 and for Inhibition of Fas-induced Apoptosis.
S-labeled procaspase-8, procaspase-8 domain (DED), procaspase-10, and FADD proteins were incubated with 10 µg of either GST or GST-BAR-DED (residues 167-358) recombinant proteins.
www.pnas.org /cgi/content/full/97/6/2597   (5203 words)

  
 PEA-15 Modulates TNF{alpha} Intracellular Signaling in Astrocytes -- SHARIF et al. 1010 (1): 43 -- Annals of the New ...
Knock-out of the neural death effector domain protein PEA-15 demonstrates that its expression protects astrocytes from TNFalpha-induced apoptosis.
The death effector domain of PEA-15 is involved in its regulation of integrin activation.
Death effector domain protein PEA-15 potentiates Ras activation of extracellular signal receptor-activated kinase by an adhesion-independent mechanism.
www.annalsnyas.org /cgi/content/full/1010/1/43   (2424 words)

  
 Fas-associated Factor 1, FAF1, Is a Member of Fas Death-inducing Signaling Complex -- Ryu et al. 278 (26): 24003 -- ...
Sequence of FAF1-(302–381) with caspase-8 DEDs and FADD-DED was aligned by using the program ANTHEPROT version 6.0, and the structure of helix was analyzed by protein data base (www2.protein.Osaka-u.ac.jp).
the conventional DED domains to FAF1-(181–381) was not
among the DEDID of FAF1 and the DEDs of caspase-8 and of FADD.
www.jbc.org /cgi/content/full/278/26/24003   (4440 words)

  
 DEFT, a Novel Death Effector Domain-Containing Molecule Predominantly Expressed in Testicular Germ Cells -- Leo et al. ...
domain of the death receptor binds to the adaptor molecule Fas-associating
A, Amino acid sequence corresponding to DED of human/rat DEFT is aligned with N-terminal DEDs of human FADD, procaspase-8 and -10, and c-FLIP.
B, Phylogenetic analysis of DED motifs of DEFT, procaspases-8 and -10, c-FLIP, PEA-15, and Bap31.
endo.endojournals.org /cgi/content/full/139/12/4839   (5404 words)

  
 Homology modeling provides insights into the binding mode of the PAAD/DAPIN/pyrin domain, a fourth member of the ...
PAAD domain the fourth branch of the death domain/CARD/DED superfamily.
Aravind, L., Dixit, V.M., and Koonin, E.V. The domains of death: Evolution of the apoptosis machinery.
Martinon, F., Hofmann, K., and Tschopp, J. The pyrin domain: A possible member of the death domain-fold family implicated in apoptosis and inflammation.
www.proteinscience.org /cgi/content/full/12/9/1872   (5180 words)

  
 Mechanisms of Apoptosis -- Reed 157 (5): 1415 -- American Journal of Pathology
The domain arrangements of the known members of the human DD family are presented.
The domain arrangements of some of the known members of the DED family are presented.
The domain arrangements of the known members of the human IAP family are presented.
ajp.amjpathol.org /cgi/content/full/157/5/1415   (8849 words)

  
 The adaptor molecule FADD from Xenopus laevis demonstrates evolutionary conservation of its pro-apoptotic activity -- ...
DED domain similar to those of mammalian FADD and caspase-8.
Sakamaki, K., Miyajima, I., Kitamura and Miyajima, A. (1992) Critical cytoplasmic domains of the common ß subunit of the human GM- CSF, IL-3 and IL-5 receptors for growth signal trans-duction and tyrosine phosphorylation.
(1993) Ligand-dependent activation of chimeric receptors with the cytoplasmic domain of the interleukin-3 receptor ß subunit (ßIL3).
www.genestocellsonline.org /cgi/content/full/9/12/1249   (6527 words)

  
 The PYRIN domain: A member of the death domain-fold superfamily -- Fairbrother et al. 10 (9): 1911 -- Protein Science
Hydrophobic residues that contribute to the cores of the folded death-domain family proteins and the CARD7 PYRIN domain model, based on environment classes determined using the program Profiles-3D, are indicated in red.
For comparison, the positions of highly conserved hydrophobic residues in the PYRIN domains sequences are indicated by asterisks.
Liepinsh, E., Ilag, L.L., Otting, G., and Ibáñez, C.F. NMR structure of the death domain of the p75 neurotrophin receptor.
www.proteinscience.org /cgi/content/full/10/9/1911   (4678 words)

  
 Mammalian initiator apoptotic caspases -- Ho and Hawkins 272 (21): 5436 -- FEBS Journal   (Site not responding. Last check: 2007-10-18)
significance of this domain is exemplified by the observation
Thomas LR, Henson A, Reed JC, Salsbury FR and Thorburn A (2004) Direct binding of Fas-associated death domain (FADD) to the tumor necrosis factor-related apoptosis-inducing ligand receptor DR5 is regulated by the death effector domain of FADD.
Harper N, Hughes M, MacFarlane M and Cohen GM (2003) Fas-associated death domain protein and caspase-8 are not recruited to the tumor necrosis factor receptor 1 signaling complex during tumor necrosis factor-induced apoptosis.
content.febsjournal.org /cgi/content/full/272/21/5436   (7316 words)

  
 Death Effector Domain Protein PEA-15 Potentiates Ras Activation of Extracellular Signal Receptor-activated Kinase by an ...
DED of PEA-15 did not activate ERK, hence it is not sufficient
Ramos, J.W., Kojima, T.K., Hughes, P.E., Fenczik, C.A., and Ginsberg, M.H. The death effector domain of PEA-15 is involved in its regulation of integrin activation.
Schievella, A.R., Chen, J.H., Graham, J.R., and Lin, L.L. MADD, a novel death domain protein that interacts with the type 1 tumor necrosis factor receptor and activates mitogen-activated protein kinase.
www.molbiolcell.org /cgi/content/full/11/9/2863   (6254 words)

  
 B Cell Receptor Cross-Linking Triggers a Caspase-8- Dependent Apoptotic Pathway That Is Independent of the Death ...   (Site not responding. Last check: 2007-10-18)
B Cell Receptor Cross-Linking Triggers a Caspase-8- Dependent Apoptotic Pathway That Is Independent of the Death Effector Domain of Fas-Associated Death Domain Protein -- Besnault et al.
B Cell Receptor Cross-Linking Triggers a Caspase-8- Dependent Apoptotic Pathway That Is Independent of the Death Effector Domain of Fas-Associated Death Domain Protein
be mediated by FADD molecules devoid of DED domains.
www.jimmunol.org /cgi/content/full/167/2/733   (5852 words)

  
 Index: d
Death Domain: homologous cytoplasmic domain of Death Receptors; by using their DDs, activated death receptors recruit adaptor molecules like FADD, TRADD or DAXX, which eventually mediate the apoptotic signal to the apoptotic machinery.
Death Effector Domain: the DED is a specific example of a more global homophilic interaction domain termed CARD, which is found in several caspases with large prodomains.
DED-Recruiting Domain; a domain of modest homology to the DED domain, DRD was found in FLASH, which binds to the DEDs of DADD and caspase-8.
www.celldeath.de /encyclo/index/d.htm   (938 words)

  
 NCBI CDD cd00045
DED is part of a superfamily of death domains which also includes death-domain (DD) and caspase recruitment domain (CARD).
Caspases are the primary executioners of apoptosis via proteolytic cascades, and upstream caspases such as caspase-8 and caspase-9 are activated by signaling complexes such as the death inducing signaling complex (DISC) and the apoptosome.
Binding of caspases to specific adaptor molecules via DED or CARD domains leads to autoactivation of caspases.
www.ncbi.nlm.nih.gov /Structure/cdd/cddsrv.cgi?uid=cd00045   (116 words)

  
 Comparative Analysis of Apoptosis and Inflammation Genes of Mice and Humans -- Reed et al. 13 (6): 1376 -- Genome ...
domains of interest, which were not recognized previously.
This domain is commonly implicated in regulation of Caspases
Lugovskoy, A., Zhou, P., Chou, J., McCarty, J., Li, P., and Wagner, G. Solution structure of the cide-n domain of cide-b and a model for cide-n/cide-n interactions in the DNA fragmentation pathway of apoptosis.
www.genome.org /cgi/content/full/13/6b/1376   (6639 words)

  
 Proteases for Cell Suicide: Functions and Regulation of Caspases -- Chang and Yang 64 (4): 821 -- Microbiology and ...
All mammalian caspases are of human origin except for murine caspase-11 and -12, for which no human counterparts have been identified yet.
Phylogenetic relationships are based on sequence similarity among the protease domains.
single globular domain, and the core of the globular domain is
mmbr.asm.org /cgi/content/full/64/4/821   (9427 words)

  
 Dysregulation of Apoptosis in Cancer -- Reed 17 (9): 2941 -- Journal of Clinical Oncology
domain, that is responsible for recruiting adapter proteins
Upon bind trimeric Fas ligand, Fas molecules are clustered at the plasma membrane, which results in recruitment of adapter proteins such as Fadd/Mort-1 via death domain (DD) interactions.
Fadd/Mort-1 binds via DED domain interactions to caspase-8, and possibly caspase-10 (not shown), inducing proteolytic activation to p20 and p10 subunits and removing the N-terminal DED-containing prodomain.
www.jco.org /cgi/content/full/17/9/2941   (7169 words)

  
 CLARP, a death effector domain-containing protein interacts with caspase-8 and regulates apoptosis -- Inohara et al. ...
domain that are predicted to be required for proteolysis were
E8 protein of equine herpesvirus-2 (1360817), and DED of FADD
DEDs and CLD are shown in box I and box II, respectively.
www.pnas.org /cgi/content/full/94/20/10717   (4628 words)

  
 [No title]
Cell death signals are transduced by death domain (DD) death effector domain (DED), and caspase recruitment domain (CARD) containing molecules.
Several molecules including caspases and adaptor FADD contain DEDs.
A novel protein that interacts with DED of caspase-8 and —10, and FADD was identified recently and designated DEDAF for DED associated factor (1).
www.eurogentec.com /module/FileLib/2227PR.doc   (463 words)

  
 GeneCard for DEDD2
Search for antibodies at Abcam and the World's Antibody Gateway (free search engine of over 150 antibody companies).
Graphical View of Domain Structure for UniProt Entry Q8WXF8
Domain: Interactions with CASP8 and CASP10 are mediated by the DED domain.
www.genecards.org /cgi-bin/carddisp.pl?gene=DEDD2   (749 words)

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