1rk8
From Proteopedia
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<StructureSection load='1rk8' size='340' side='right'caption='[[1rk8]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1rk8' size='340' side='right'caption='[[1rk8]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1rk8]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1rk8]] is a 3 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=1RK8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RK8 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | |
| - | <tr id=' | + | |
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rk8 OCA], [https://pdbe.org/1rk8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rk8 RCSB], [https://www.ebi.ac.uk/pdbsum/1rk8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rk8 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=1rk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rk8 OCA], [https://pdbe.org/1rk8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rk8 RCSB], [https://www.ebi.ac.uk/pdbsum/1rk8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rk8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/MGN_DROME MGN_DROME] Participates in the bidirectional intercellular signaling between the posterior follicle cells and oocyte to establish spatial coordinates that induces axis formation. Complex with tsu is essential for cytoplasmic localization of oskar in the posterior pole of oocytes. Required for the polarization of the oocyte microtubule cytoskeleton.<ref>PMID:8026338</ref> <ref>PMID:9272960</ref> <ref>PMID:9210377</ref> <ref>PMID:12730685</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1rk8 ConSurf]. | </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=1rk8 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The exon junction complex (EJC) is deposited on mRNAs as a consequence of splicing and influences postsplicing mRNA metabolism. The Mago-Y14 heterodimer is a core component of the EJC. Recently, the protein PYM has been identified as an interacting partner of Mago-Y14. Here we show that PYM is a cytoplasmic RNA-binding protein that is excluded from the nucleus by Crm1. PYM interacts directly with Mago-Y14 by means of its N-terminal domain. The crystal structure of the Drosophila ternary complex at 1.9 A resolution reveals that PYM binds Mago and Y14 simultaneously, capping their heterodimerization interface at conserved surface residues. Formation of this ternary complex is also observed with the human proteins. Mago residues involved in the interaction with PYM have been implicated in nonsense-mediated mRNA decay (NMD). Consistently, human PYM is active in NMD tethering assays. Together, these data suggest a role for PYM in NMD. | ||
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| - | Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex.,Bono F, Ebert J, Unterholzner L, Guttler T, Izaurralde E, Conti E EMBO Rep. 2004 Mar;5(3):304-10. Epub 2004 Feb 13. PMID:14968132<ref>PMID:14968132</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1rk8" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Drosophila melanogaster]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Bono | + | [[Category: Bono F]] |
| - | [[Category: Conti | + | [[Category: Conti E]] |
| - | [[Category: Ebert | + | [[Category: Ebert J]] |
| - | [[Category: Guettler | + | [[Category: Guettler T]] |
| - | [[Category: Izaurralde | + | [[Category: Izaurralde E]] |
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Current revision
Structure of the cytosolic protein PYM bound to the Mago-Y14 core of the exon junction complex
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