3b31: Difference between revisions

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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=3b31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b31 OCA], [https://pdbe.org/3b31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b31 RCSB], [https://www.ebi.ac.uk/pdbsum/3b31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b31 ProSAT]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

Internal ribosome entry site (IRES) RNAs initiate protein synthesis in eukaryotic cells by a noncanonical cap-independent mechanism. IRESes are critical for many pathogenic viruses, but efforts to understand their function are complicated by the diversity of IRES sequences as well as by limited high-resolution structural information. The intergenic region (IGR) IRESes of the Dicistroviridae viruses are powerful model systems to begin to understand IRES function. Here we present the crystal structure of a Dicistroviridae IGR IRES domain that interacts with the ribosome's decoding groove. We find that this RNA domain precisely mimics the transfer RNA anticodon-messenger RNA codon interaction, and its modeled orientation on the ribosome helps explain translocation without peptide bond formation. When combined with a previous structure, this work completes the first high-resolution description of an IRES RNA and provides insight into how RNAs can manipulate complex biological machines.

tRNA-mRNA mimicry drives translation initiation from a viral IRES.,Costantino DA, Pfingsten JS, Rambo RP, Kieft JS Nat Struct Mol Biol. 2008 Jan;15(1):57-64. Epub 2007 Dec 23. PMID:18157151<ref>PMID:18157151</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

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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=3b31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b31 OCA], [https://pdbe.org/3b31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b31 RCSB], [https://www.ebi.ac.uk/pdbsum/3b31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b31 ProSAT]</span></td></tr>
 </table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Internal ribosome entry site (IRES) RNAs initiate protein synthesis in eukaryotic cells by a noncanonical cap-independent mechanism. IRESes are critical for many pathogenic viruses, but efforts to understand their function are complicated by the diversity of IRES sequences as well as by limited high-resolution structural information. The intergenic region (IGR) IRESes of the Dicistroviridae viruses are powerful model systems to begin to understand IRES function. Here we present the crystal structure of a Dicistroviridae IGR IRES domain that interacts with the ribosome's decoding groove. We find that this RNA domain precisely mimics the transfer RNA anticodon-messenger RNA codon interaction, and its modeled orientation on the ribosome helps explain translocation without peptide bond formation. When combined with a previous structure, this work completes the first high-resolution description of an IRES RNA and provides insight into how RNAs can manipulate complex biological machines.
+tRNA-mRNA mimicry drives translation initiation from a viral IRES.,Costantino DA, Pfingsten JS, Rambo RP, Kieft JS Nat Struct Mol Biol. 2008 Jan;15(1):57-64. Epub 2007 Dec 23. PMID:18157151<ref>PMID:18157151</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3b31" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>