2o71
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
- | + | ==Crystal structure of RAIDD DD== | |
- | === | + | <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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O71 FirstGlance]. <br> | |
- | ==Disease== | + | </td></tr><tr><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 Homo sapiens])</td></tr> |
- | [[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> | + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o71 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2o71 RCSB], [http://www.ebi.ac.uk/pdbsum/2o71 PDBsum]</span></td></tr> |
- | + | <table> | |
- | ==Function== | + | == 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> | ||
+ | == 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/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/chain_selection.php?pdb_ID=2ata 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> | |
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Park, H.]] | [[Category: Park, H.]] |
Revision as of 18:00, 30 September 2014
Crystal structure of RAIDD DD
|
Categories: Homo sapiens | Park, H. | Wu, H. | Apoptosis | Death domain | Raidd