2hua

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Revision as of 18:28, 29 January 2008

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Solution Structure of CSFV IRES Domain IIa

Overview

Internal ribosome entry site (IRES) RNAs from the hepatitis C virus (HCV), and classical swine fever virus (CSFV) coordinate cap-independent assembly, of eukaryotic 48S initiation complexes, consisting of the 40S ribosomal, subunit, eukaryotic initiation factor (eIF) 3 and the, eIF2/GTP/Met-tRNA(i)(Met) ternary complex. Here, we report that these, IRESes also play a functional role during 80S ribosome assembly downstream, of 48S complex formation, in promoting eIF5-induced GTP hydrolysis and, eIF2/GDP release from the initiation complex. We show that this function, is encoded in their independently folded IRES domain II and that it, depends both on its characteristic bent conformation and two conserved RNA, motifs, an apical hairpin loop and a loop E. Our data suggest a general, mode of subunit joining in HCV and HCV-like IRESes.

About this Structure

2HUA is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

Reference

HCV and CSFV IRES domain II mediate eIF2 release during 80S ribosome assembly., Locker N, Easton LE, Lukavsky PJ, EMBO J. 2007 Feb 7;26(3):795-805. Epub 2007 Jan 25. PMID:17255934

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