Structural highlights
Publication Abstract from PubMed
Canonical cap-dependent translation initiation requires a large number of protein factors that act in a stepwise assembly process. In contrast, internal ribosomal entry sites (IRESs) are cis-acting RNAs that in some cases completely supplant these factors by recruiting and activating the ribosome using a single structured RNA. Here we present the crystal structures of the ribosome-binding domain from a Dicistroviridae intergenic region IRES at 3.1 angstrom resolution, providing a view of the prefolded architecture of an all-RNA translation initiation apparatus. Docking of the structure into cryo-electron microscopy reconstructions of an IRES-ribosome complex suggests a model for ribosome manipulation by a dynamic IRES RNA.
Structural basis for ribosome recruitment and manipulation by a viral IRES RNA.,Pfingsten JS, Costantino DA, Kieft JS Science. 2006 Dec 1;314(5804):1450-4. Epub 2006 Nov 23. PMID:17124290[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pfingsten JS, Costantino DA, Kieft JS. Structural basis for ribosome recruitment and manipulation by a viral IRES RNA. Science. 2006 Dec 1;314(5804):1450-4. Epub 2006 Nov 23. PMID:17124290 doi:http://dx.doi.org/1133281