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2xes

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[[Image:2xes.png|left|200px]]
 
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==Human PatL1 C-terminal domain (loop variant)==
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The line below this paragraph, containing "STRUCTURE_2xes", creates the "Structure Box" on the page.
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<StructureSection load='2xes' size='340' side='right'caption='[[2xes]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2xes]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XES FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_2xes| PDB=2xes | SCENE= }}
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2xeq|2xeq]], [[2xer|2xer]]</div></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xes FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xes OCA], [https://pdbe.org/2xes PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xes RCSB], [https://www.ebi.ac.uk/pdbsum/2xes PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xes ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/PATL1_HUMAN PATL1_HUMAN]] RNA-binding protein involved in deadenylation-dependent decapping of mRNAs, leading to the degradation of mRNAs. Acts as a scaffold protein that connects deadenylation and decapping machinery. Required for cytoplasmic mRNA processing body (P-body) assembly. In case of infection, required for translation and replication of hepatitis C virus (HCV).<ref>PMID:17936923</ref> <ref>PMID:19628699</ref> <ref>PMID:20584987</ref> <ref>PMID:20852261</ref> <ref>PMID:20543818</ref>
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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/xe/2xes_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/main_output.php?pdb_ID=2xes 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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Pat proteins regulate the transition of mRNAs from a state that is translationally active to one that is repressed, committing targeted mRNAs to degradation. Pat proteins contain a conserved N-terminal sequence, a proline-rich region, a Mid domain and a C-terminal domain (Pat-C). We show that Pat-C is essential for the interaction with mRNA decapping factors (i.e. DCP2, EDC4 and LSm1-7), whereas the P-rich region and Mid domain have distinct functions in modulating these interactions. DCP2 and EDC4 binding is enhanced by the P-rich region and does not require LSm1-7. LSm1-7 binding is assisted by the Mid domain and is reduced by the P-rich region. Structural analysis revealed that Pat-C folds into an alpha-alpha superhelix, exposing conserved and basic residues on one side of the domain. This conserved and basic surface is required for RNA, DCP2, EDC4 and LSm1-7 binding. The multiplicity of interactions mediated by Pat-C suggests that certain of these interactions are mutually exclusive and, therefore, that Pat proteins switch decapping partners allowing transitions between sequential steps in the mRNA decapping pathway.
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===HUMAN PATL1 C-TERMINAL DOMAIN (LOOP VARIANT)===
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The C-terminal alpha-alpha superhelix of Pat is required for mRNA decapping in metazoa.,Braun JE, Tritschler F, Haas G, Igreja C, Truffault V, Weichenrieder O, Izaurralde E EMBO J. 2010 Jul 21;29(14):2368-80. Epub 2010 Jun 11. PMID:20543818<ref>PMID:20543818</ref>
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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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The line below this paragraph, {{ABSTRACT_PUBMED_20543818}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2xes" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20543818 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20543818}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Human]]
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[[2xes]] is a 2 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=2XES OCA].
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[[Category: Large Structures]]
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[[Category: Tritschler, F]]
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==Reference==
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[[Category: Weichenrieder, O]]
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<ref group="xtra">PMID:020543818</ref><references group="xtra"/>
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[[Category: Mrna decapping]]
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[[Category: Homo sapiens]]
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[[Category: P-body]]
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[[Category: Tritschler, F.]]
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[[Category: Rna binding protein]]
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[[Category: Weichenrieder, O.]]
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Current revision

Human PatL1 C-terminal domain (loop variant)

PDB ID 2xes

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