2o71
From Proteopedia
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| - | {{STRUCTURE_2o71| PDB=2o71 | SCENE= }} | ||
| - | ===Crystal structure of RAIDD DD=== | ||
| - | {{ABSTRACT_PUBMED_16434054}} | ||
| - | == | + | ==Crystal structure of RAIDD DD== |
| - | [[http://www.uniprot.org/uniprot/CRADD_HUMAN CRADD_HUMAN | + | <StructureSection load='2o71' size='340' side='right'caption='[[2o71]], [[Resolution|resolution]] 2.00Å' scene=''> |
| + | == Structural highlights == | ||
| + | <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='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> | ||
| + | </table> | ||
| + | == 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> | ||
| + | == 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. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/2o71_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2o71 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:16434054</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2o71" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | < | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Park H]] |
| - | [[Category: | + | [[Category: Wu H]] |
| - | + | ||
| - | + | ||
Current revision
Crystal structure of RAIDD DD
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