View source for 2vxg


==Crystal structure of the conserved C-terminal region of Ge-1==
<StructureSection load='2vxg' size='340' side='right'caption='[[2vxg]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2vxg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VXG 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]] 1.9&#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=2vxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vxg OCA], [https://pdbe.org/2vxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vxg RCSB], [https://www.ebi.ac.uk/pdbsum/2vxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vxg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/EDC4_DROME EDC4_DROME] In the process of mRNA degradation, seems to play a role in mRNA decapping. Required for silencing a subset of endogenous miRNA targets.<ref>PMID:17901217</ref> 
== 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/vx/2vxg_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=2vxg ConSurf].
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== Publication Abstract from PubMed ==
The removal of the 5' cap structure by the DCP1-DCP2 decapping complex irreversibly commits eukaryotic mRNAs to degradation. In human cells, the interaction between DCP1 and DCP2 is bridged by the Ge-1 protein. Ge-1 contains an N-terminal WD40-repeat domain connected by a low-complexity region to a conserved C-terminal domain. It was reported that the C-terminal domain interacts with DCP2 and mediates Ge-1 oligomerization and P-body localization. To understand the molecular basis for these functions, we determined the three-dimensional crystal structure of the most conserved region of the Drosophila melanogaster Ge-1 C-terminal domain. The region adopts an all alpha-helical fold related to ARM- and HEAT-repeat proteins. Using structure-based mutants we identified an invariant surface residue affecting P-body localization. The conservation of critical surface and structural residues suggests that the C-terminal region adopts a similar fold with conserved functions in all members of the Ge-1 protein family.

The C-terminal region of Ge-1 presents conserved structural features required for P-body localization.,Jinek M, Eulalio A, Lingel A, Helms S, Conti E, Izaurralde E RNA. 2008 Oct;14(10):1991-8. Epub 2008 Aug 28. PMID:18755833<ref>PMID:18755833</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Conti E]]
[[Category: Eulalio A]]
[[Category: Helms S]]
[[Category: Izaurralde E]]
[[Category: Jinek M]]
[[Category: Lingel A]]