2nc0
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2nc0 is ON HOLD until Paper Publication Authors: Imai, S., D'Souza, V., Wagner, G. Description: Solution structure of the St domain of EMCV IRES [[...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution structure of the St domain of EMCV IRES== | |
| + | <StructureSection load='2nc0' size='340' side='right'caption='[[2nc0]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2nc0]] 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=2NC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NC0 FirstGlance]. <br> | ||
| + | </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=2nc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nc0 OCA], [https://pdbe.org/2nc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nc0 RCSB], [https://www.ebi.ac.uk/pdbsum/2nc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nc0 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 2nc0" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: D'Souza V]] | ||
| + | [[Category: Imai S]] | ||
| + | [[Category: Wagner G]] | ||
Current revision
Solution structure of the St domain of EMCV IRES
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