2way: Difference between revisions

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-{{Seed}}
-[[Image:2way.jpg|left|200px]]
-<!--
+==Structure of the human DDX6 C-terminal domain in complex with an EDC3- FDF peptide==
-The line below this paragraph, containing "STRUCTURE_2way", creates the "Structure Box" on the page.
+<StructureSection load='2way' size='340' side='right'caption='[[2way]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2way]] is a 4 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=2WAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WAY FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-{{STRUCTURE_2way|  PDB=2way  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2way FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2way OCA], [https://pdbe.org/2way PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2way RCSB], [https://www.ebi.ac.uk/pdbsum/2way PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2way ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/DDX6_HUMAN DDX6_HUMAN] Note=A chromosomal aberration involving DDX6 may be a cause of hematopoietic tumors such as B-cell lymphomas. Translocation t(11;14)(q23;q32).
+== Function ==
+[https://www.uniprot.org/uniprot/DDX6_HUMAN DDX6_HUMAN] In the process of mRNA degradation, may play a role in mRNA decapping.
+== 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/wa/2way_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=2way ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The DEAD box helicase DDX6/Me31B functions in translational repression and mRNA decapping. How particular RNA helicases are recruited specifically to distinct functional complexes is poorly understood. We present the crystal structure of the DDX6 C-terminal RecA-like domain bound to a highly conserved FDF sequence motif in the decapping activator EDC3. The FDF peptide adopts an alpha-helical conformation upon binding to DDX6, occupying a shallow groove opposite to the DDX6 surface involved in RNA binding and ATP hydrolysis. Mutagenesis of Me31B shows the relevance of the FDF interaction surface both for Me31B's accumulation in P bodies and for its ability to repress the expression of bound mRNAs. The translational repressor Tral contains a similar FDF motif. Together with mutational and competition studies, the structure reveals why the interactions of Me31B with EDC3 and Tral are mutually exclusive and how the respective decapping and translational repressor complexes might hook onto an mRNA substrate.
-===STRUCTURE OF THE HUMAN DDX6 C-TERMINAL DOMAIN IN COMPLEX WITH AN EDC3-FDF PEPTIDE===
+Structural basis for the mutually exclusive anchoring of P body components EDC3 and Tral to the DEAD box protein DDX6/Me31B.,Tritschler F, Braun JE, Eulalio A, Truffault V, Izaurralde E, Weichenrieder O Mol Cell. 2009 Mar 13;33(5):661-8. PMID:19285948<ref>PMID:19285948</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2way" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_19285948}}, adds the Publication Abstract to the page
+*[[Helicase 3D structures|Helicase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 19285948 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_19285948}}
+__TOC__
+</StructureSection>
-==About this Structure==
-WAY is a 4 chains structure of sequences 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=2WAY OCA].
-==Reference==
-<ref group="xtra">PMID:19285948</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Tritschler, F.]]
+[[Category: Large Structures]]
-[[Category: Weichenrieder, O.]]
+[[Category: Tritschler F]]
-[[Category: Atp-binding]]
+[[Category: Weichenrieder O]]
-[[Category: Atp-dependent rna helicase]]
-[[Category: Chromosomal rearrangement]]
-[[Category: Cytoplasm]]
-[[Category: Dead-box protein]]
-[[Category: Decapping]]
-[[Category: Helicase]]
-[[Category: Hydrolase]]
-[[Category: Mirna]]
-[[Category: Mrna decay]]
-[[Category: Nucleotide-binding]]
-[[Category: P-body]]
-[[Category: P54]]
-[[Category: Phosphoprotein]]
-[[Category: Proto-oncogene]]
-[[Category: Rck]]
-[[Category: Rna-binding]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 25 12:13:02 2009''