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<StructureSection load='3qwx' size='340' side='right'caption='[[3qwx]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
<StructureSection load='3qwx' size='340' side='right'caption='[[3qwx]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3qwx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QWX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QWX FirstGlance]. <br>
<table><tr><td colspan='2'>[[3qwx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QWX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QWX FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.01&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3qwy|3qwy]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ced-2, Y41D4B.13 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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=3qwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qwx OCA], [https://pdbe.org/3qwx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qwx RCSB], [https://www.ebi.ac.uk/pdbsum/3qwx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qwx 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=3qwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qwx OCA], [https://pdbe.org/3qwx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qwx RCSB], [https://www.ebi.ac.uk/pdbsum/3qwx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qwx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CED2_CAEEL CED2_CAEEL]] Required for cell migration and engulfment of cell corpses but not for programmed cell death/apoptosis. Has a role in the migration of the 2 gonadal distal tip cells (DTCs).<ref>PMID:10707082</ref> <ref>PMID:11449278</ref> <ref>PMID:15744306</ref> <ref>PMID:1936965</ref> <ref>PMID:19402756</ref> <ref>PMID:6857247</ref> 
[https://www.uniprot.org/uniprot/CED2_CAEEL CED2_CAEEL] Required for cell migration and engulfment of cell corpses but not for programmed cell death/apoptosis. Has a role in the migration of the 2 gonadal distal tip cells (DTCs).<ref>PMID:10707082</ref> <ref>PMID:11449278</ref> <ref>PMID:15744306</ref> <ref>PMID:1936965</ref> <ref>PMID:19402756</ref> <ref>PMID:6857247</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In the nematode Caenorhabditis elegans, the cell corpse engulfment proteins CED-2, CED-5, and CED-12 act in the same pathway to regulate the activation of the Rac small GTPase, CED-10, leading to the rearrangement of the actin cytoskeleton for engulfing apoptotic cells. Nevertheless, it is not well understood how these proteins act together. Here we report the crystal structures of the CED-2 protein as determined by X-ray crystallography. The full-length CED-2 protein and its truncated form containing the N-terminal SH2 domain and the first SH3 domain show similar three-dimensional structures. A CED-2 point mutation (F125G) disrupting its interaction with the PXXP motif of CED-5 did not affect its rescuing activity. However, CED-2 was found to interact with the N-terminal region of CED-5. Our findings suggest that CED-2 may regulate cell corpse engulfment by interacting with CED-5 through the N-terminal region rather than the PXXP motif.
 
Crystal structure of the cell corpse engulfment protein CED-2 in Caenorhabditis elegans.,Kang Y, Xu J, Liu Y, Sun J, Sun D, Hu Y, Liu Y Biochem Biophys Res Commun. 2011 May 17. PMID:21616056<ref>PMID:21616056</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3qwx" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Caeel]]
[[Category: Caenorhabditis elegans]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kang, Y]]
[[Category: Kang Y]]
[[Category: Liu, Y]]
[[Category: Liu Y]]
[[Category: Sun, J]]
[[Category: Sun J]]
[[Category: Cell engulfment]]
[[Category: Signaling protein]]

Latest revision as of 10:50, 21 February 2024

CED-2 1-174

3qwx, resolution 2.01Å

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