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2nby

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'''Unreleased structure'''
 
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The entry 2nby is ON HOLD until Paper Publication
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==Solution structure of the J domain of EMCV IRES==
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<StructureSection load='2nby' size='340' side='right'caption='[[2nby]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2nby]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NBY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NBY FirstGlance]. <br>
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</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=2nby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nby OCA], [https://pdbe.org/2nby PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nby RCSB], [https://www.ebi.ac.uk/pdbsum/2nby PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nby ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Many viruses bypass canonical cap-dependent translation in host cells by using internal ribosomal entry sites (IRESs) in their transcripts; IRESs hijack initiation factors for the assembly of initiation complexes. However, it is currently unknown how IRES RNAs recognize initiation factors that have no endogenous RNA binding partners; in a prominent example, the IRES of encephalomyocarditis virus (EMCV) interacts with the HEAT-1 domain of eukaryotic initiation factor 4G (eIF4G). Here we report the solution structure of the J-K region of this IRES and show that its stems are precisely organized to position protein-recognition bulges. This multisite interaction mechanism operates on an all-or-nothing principle in which all domains are required. This preorganization is accomplished by an 'adjuster module': a pentaloop motif that acts as a dual-sided docking station for base-pair receptors. Because subtle changes in the orientation abrogate protein capture, our study highlights how a viral RNA acquires affinity for a target protein.
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Authors: Imai, S., D'Souza, V., Wagner, G.
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An accurately preorganized IRES RNA structure enables eIF4G capture for initiation of viral translation.,Imai S, Kumar P, Hellen CU, D'Souza VM, Wagner G Nat Struct Mol Biol. 2016 Sep;23(9):859-64. doi: 10.1038/nsmb.3280. Epub 2016 Aug, 15. PMID:27525590<ref>PMID:27525590</ref>
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Description: Solution structure of the J domain of EMCV IRES
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Imai, S]]
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<div class="pdbe-citations 2nby" style="background-color:#fffaf0;"></div>
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[[Category: Wagner, G]]
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== References ==
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[[Category: D'Souza, V]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Synthetic construct]]
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[[Category: D'Souza V]]
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[[Category: Imai S]]
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[[Category: Wagner G]]

Current revision

Solution structure of the J domain of EMCV IRES

PDB ID 2nby

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