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2of5

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Revision as of 12:55, 9 June 2021

Oligomeric Death Domain complex

Structural highlights

2of5 is a 12 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	CRADD, RAIDD (HUMAN), LRDD, PIDD (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[CRADD_HUMAN] Defects in CRADD are the cause of mental retardation autosomal recessive type 34 (MRT34) [MIM:614499]. A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. MRT34 is a non-syndromic form. Affected individuals have mildly delayed development and significantly impaired cognitive function, precluding independent living and self-care. Speech is rudimentary, but articulate; autism is not present.^[1]

Function

[CRADD_HUMAN] Apoptotic adaptor molecule specific for caspase-2 and FASL/TNF receptor-interacting protein RIP. In the presence of RIP and TRADD, CRADD recruits caspase-2 to the TNFR-1 signalling complex. [PIDD_HUMAN] Promotes apoptosis downstream of the tumor suppressor as component of the DNA damage/stress response pathway that connects p53/TP53 to apoptosis. Associates with NEMO/IKBKG and RIP1 and enhances sumoylation and ubiquitination of NEMO/IKBKG which is important for activation of the transcription factor NF-kappa-B. Associates with CASP2/caspase-2 and CRADD/RAIDD, and induces activation of CASP2 which an important regulator in apoptotic pathways.^[2] ^[3] ^[4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Proteins of the death domain (DD) superfamily mediate assembly of oligomeric signaling complexes for the activation of caspases and kinases via unknown mechanisms. Here we report the crystal structure of the PIDD DD and RAIDD DD complex, which forms the core of the caspase-2-activating complex PIDDosome. Although RAIDD DD and PIDD DD are monomers, they assemble into a complex that comprises seven RAIDD DDs and five PIDD DDs. Despite the use of an asymmetric assembly mechanism, all DDs in the complex are in quasi-equivalent environments. The structure provided eight unique asymmetric interfaces, which can be classified into three types. These three types of interactions together cover a majority of the DD surface. Mutagenesis on almost all interfaces leads to disruption of the assembly, resulting in defective caspase-2 activation. The three types of interactions may represent most, if not all, modes of interactions in the DD superfamily for assembling complexes of different stoichiometry.

Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex.,Park HH, Logette E, Raunser S, Cuenin S, Walz T, Tschopp J, Wu H Cell. 2007 Feb 9;128(3):533-46. PMID:17289572^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Puffenberger EG, Jinks RN, Sougnez C, Cibulskis K, Willert RA, Achilly NP, Cassidy RP, Fiorentini CJ, Heiken KF, Lawrence JJ, Mahoney MH, Miller CJ, Nair DT, Politi KA, Worcester KN, Setton RA, Dipiazza R, Sherman EA, Eastman JT, Francklyn C, Robey-Bond S, Rider NL, Gabriel S, Morton DH, Strauss KA. Genetic mapping and exome sequencing identify variants associated with five novel diseases. PLoS One. 2012;7(1):e28936. doi: 10.1371/journal.pone.0028936. Epub 2012 Jan 17. PMID:22279524 doi:10.1371/journal.pone.0028936
↑ Lin Y, Ma W, Benchimol S. Pidd, a new death-domain-containing protein, is induced by p53 and promotes apoptosis. Nat Genet. 2000 Sep;26(1):122-7. PMID:10973264 doi:10.1038/79102
↑ Tinel A, Tschopp J. The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress. Science. 2004 May 7;304(5672):843-6. Epub 2004 Apr 8. PMID:15073321 doi:10.1126/science.1095432
↑ Janssens S, Tinel A, Lippens S, Tschopp J. PIDD mediates NF-kappaB activation in response to DNA damage. Cell. 2005 Dec 16;123(6):1079-92. PMID:16360037 doi:S0092-8674(05)01042-1
↑ Park HH, Logette E, Raunser S, Cuenin S, Walz T, Tschopp J, Wu H. Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex. Cell. 2007 Feb 9;128(3):533-46. PMID:17289572 doi:10.1016/j.cell.2007.01.019

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2of5"

@@ Line 1: / Line 1: @@
 ==Oligomeric Death Domain complex==
-<StructureSection load='2of5' size='340' side='right' caption='[[2of5]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
+<StructureSection load='2of5' size='340' side='right'caption='[[2of5]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2of5]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OF5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OF5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2of5]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OF5 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CRADD, RAIDD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), LRDD, PIDD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CRADD, RAIDD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), LRDD, PIDD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2of5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2of5 OCA], [http://pdbe.org/2of5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2of5 RCSB], [http://www.ebi.ac.uk/pdbsum/2of5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2of5 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2of5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2of5 OCA], [https://pdbe.org/2of5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2of5 RCSB], [https://www.ebi.ac.uk/pdbsum/2of5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2of5 ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/CRADD_HUMAN CRADD_HUMAN]] Defects in CRADD are the cause of mental retardation autosomal recessive type 34 (MRT34) [MIM:[http://omim.org/entry/614499 614499]]. A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. MRT34 is a non-syndromic form. Affected individuals have mildly delayed development and significantly impaired cognitive function, precluding independent living and self-care. Speech is rudimentary, but articulate; autism is not present.<ref>PMID:22279524</ref>
+[[https://www.uniprot.org/uniprot/CRADD_HUMAN CRADD_HUMAN]] Defects in CRADD are the cause of mental retardation autosomal recessive type 34 (MRT34) [MIM:[https://omim.org/entry/614499 614499]]. A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. MRT34 is a non-syndromic form. Affected individuals have mildly delayed development and significantly impaired cognitive function, precluding independent living and self-care. Speech is rudimentary, but articulate; autism is not present.<ref>PMID:22279524</ref>
 == Function ==
-[[http://www.uniprot.org/uniprot/CRADD_HUMAN CRADD_HUMAN]] Apoptotic adaptor molecule specific for caspase-2 and FASL/TNF receptor-interacting protein RIP. In the presence of RIP and TRADD, CRADD recruits caspase-2 to the TNFR-1 signalling complex. [[http://www.uniprot.org/uniprot/PIDD_HUMAN PIDD_HUMAN]] Promotes apoptosis downstream of the tumor suppressor as component of the DNA damage/stress response pathway that connects p53/TP53 to apoptosis. Associates with NEMO/IKBKG and RIP1 and enhances sumoylation and ubiquitination of NEMO/IKBKG which is important for activation of the transcription factor NF-kappa-B. Associates with CASP2/caspase-2 and CRADD/RAIDD, and induces activation of CASP2 which an important regulator in apoptotic pathways.<ref>PMID:10973264</ref> <ref>PMID:15073321</ref> <ref>PMID:16360037</ref>
+[[https://www.uniprot.org/uniprot/CRADD_HUMAN CRADD_HUMAN]] Apoptotic adaptor molecule specific for caspase-2 and FASL/TNF receptor-interacting protein RIP. In the presence of RIP and TRADD, CRADD recruits caspase-2 to the TNFR-1 signalling complex. [[https://www.uniprot.org/uniprot/PIDD_HUMAN PIDD_HUMAN]] Promotes apoptosis downstream of the tumor suppressor as component of the DNA damage/stress response pathway that connects p53/TP53 to apoptosis. Associates with NEMO/IKBKG and RIP1 and enhances sumoylation and ubiquitination of NEMO/IKBKG which is important for activation of the transcription factor NF-kappa-B. Associates with CASP2/caspase-2 and CRADD/RAIDD, and induces activation of CASP2 which an important regulator in apoptotic pathways.<ref>PMID:10973264</ref> <ref>PMID:15073321</ref> <ref>PMID:16360037</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 35: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Cuenin, S]]
 [[Category: Logette, E]]

2of5

From Proteopedia

Revision as of 12:55, 9 June 2021

Oligomeric Death Domain complex

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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