|
|
| Line 3: |
Line 3: |
| | <StructureSection load='2o71' size='340' side='right'caption='[[2o71]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='2o71' size='340' side='right'caption='[[2o71]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2o71]] is a 1 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=2O71 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O71 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2o71]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O71 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O71 FirstGlance]. <br> |
| - | </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])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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=2o71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o71 OCA], [https://pdbe.org/2o71 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o71 RCSB], [https://www.ebi.ac.uk/pdbsum/2o71 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o71 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=2o71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o71 OCA], [https://pdbe.org/2o71 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o71 RCSB], [https://www.ebi.ac.uk/pdbsum/2o71 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o71 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[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>
| + | [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 == | | == Function == |
| - | [[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/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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 34: |
Line 34: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Park, H]] | + | [[Category: Park H]] |
| - | [[Category: Wu, H]] | + | [[Category: Wu H]] |
| - | [[Category: Apoptosis]]
| + | |
| - | [[Category: Death domain]]
| + | |
| - | [[Category: Raidd]]
| + | |
| Structural highlights
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.
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
Caspase-2 is implicated in stress-induced apoptosis that acts as an upstream initiator of mitochondrial permeabilization. Recent studies have shown that caspase-2 activation requires a molecular complex known as the PIDDosome comprising the p53-inducible protein PIDD, the adapter protein RAIDD and caspase-2. RAIDD has an N-terminal caspase recruitment domain (CARD) that interacts with the CARD of caspase-2 and a C-terminal death domain (DD) that interacts with the DD in PIDD. As a first step towards elucidating the molecular mechanisms of caspase-2 activation, we report the crystal structure of RAIDD DD at 2.0 A resolution. The high-resolution structure reveals important features of RAIDD DD that may be important for DD folding and dynamics and for assembly of the PIDDosome.
Crystal structure of RAIDD death domain implicates potential mechanism of PIDDosome assembly.,Park HH, Wu H J Mol Biol. 2006 Mar 24;357(2):358-64. Epub 2006 Jan 11. PMID:16434054[2]
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
- ↑ Park HH, Wu H. Crystal structure of RAIDD death domain implicates potential mechanism of PIDDosome assembly. J Mol Biol. 2006 Mar 24;357(2):358-64. Epub 2006 Jan 11. PMID:16434054 doi:10.1016/j.jmb.2005.12.082
|
