2o71: Difference between revisions

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New page: left|200px<br /> <applet load="2o71" size="450" color="white" frame="true" align="right" spinBox="true" caption="2o71, resolution 2.0Å" /> '''Crystal structure of...
 
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[[Image:2o71.gif|left|200px]]<br />
<applet load="2o71" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2o71, resolution 2.0&Aring;" />
'''Crystal structure of RAIDD DD'''<br />


==Overview==
==Crystal structure of RAIDD DD==
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.
<StructureSection load='2o71' size='340' side='right'caption='[[2o71]], [[Resolution|resolution]] 2.00&Aring;' 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]] 2&#8491;</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.


==About this Structure==
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>
2O71 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2O71 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16434054 16434054]
</div>
<div class="pdbe-citations 2o71" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Park, H.]]
[[Category: Park H]]
[[Category: Wu, H.]]
[[Category: Wu H]]
[[Category: death domain]]
[[Category: raidd]]
 
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