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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=IRI:IRIDIUM+HEXAMMINE+ION'>IRI</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>

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== 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>

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<div class="pdbe-citations 3b31" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Costantino, D A]]

[[Category: Kieft, J S]]

[[Category: Pfingsten, J S]]

[[Category: Rambo, R P]]

[[Category: Trna mimicry]]