2agn
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(New page: 200px<br /><applet load="2agn" size="350" color="white" frame="true" align="right" spinBox="true" caption="2agn" /> '''Fitting of hepatitis C virus internal riboso...)
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Revision as of 16:01, 29 January 2008
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Fitting of hepatitis C virus internal ribosome entry site domains into the 15 A Cryo-EM map of a HCV IRES-80S ribosome (H. sapiens) complex
Overview
Initiation of translation of the hepatitis C virus (HCV) polyprotein is, driven by an internal ribosome entry site (IRES) RNA that bypasses much of, the eukaryotic translation initiation machinery. Here, single-particle, electron cryomicroscopy has been used to study the mechanism of HCV, IRES-mediated initiation. A HeLa in vitro translation system was used to, assemble human IRES-80S ribosome complexes under near physiological, conditions; these were stalled before elongation. Domain 2 of the HCV IRES, is bound to the tRNA exit site, touching the L1 stalk of the 60S subunit, suggesting a mechanism for the removal of the HCV IRES in the progression, to elongation. Domain 3 of the HCV IRES positions the initiation codon in, the ribosomal mRNA binding cleft by binding helix 28 at the head of the, 40S subunit. The comparison with the previously published binary 40S-HCV, IRES complex reveals structural rearrangements in the two pseudoknot, structures of the HCV IRES in translation initiation.
About this Structure
2AGN is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Structure of the hepatitis C Virus IRES bound to the human 80S ribosome: remodeling of the HCV IRES., Boehringer D, Thermann R, Ostareck-Lederer A, Lewis JD, Stark H, Structure. 2005 Nov;13(11):1695-706. PMID:16271893
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