2vxg

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[[Image:2vxg.png|left|200px]]
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==CRYSTAL STRUCTURE OF THE CONSERVED C-TERMINAL REGION OF GE-1==
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<StructureSection load='2vxg' size='340' side='right' caption='[[2vxg]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2vxg]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VXG FirstGlance]. <br>
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</td></tr><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=2vxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vxg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vxg RCSB], [http://www.ebi.ac.uk/pdbsum/2vxg PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vx/2vxg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_2vxg| PDB=2vxg | SCENE= }}
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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>
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===CRYSTAL STRUCTURE OF THE CONSERVED C-TERMINAL REGION OF GE-1===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_18755833}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2vxg]] is a 2 chain structure with sequence from [http://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].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:018755833</ref><references group="xtra"/>
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[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Conti, E.]]
[[Category: Conti, E.]]

Revision as of 02:20, 1 October 2014

CRYSTAL STRUCTURE OF THE CONSERVED C-TERMINAL REGION OF GE-1

2vxg, resolution 1.90Å

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