2HUA
Solution Structure of CSFV IRES Domain IIa
Summary for 2HUA
| Entry DOI | 10.2210/pdb2hua/pdb |
| Descriptor | CSFV IRES Domain IIa (1 entity in total) |
| Functional Keywords | rna hairpin, rna |
| Total number of polymer chains | 1 |
| Total formula weight | 12918.78 |
| Authors | Locker, N.,Easton, L.E.,Lukavsky, P.J. (deposition date: 2006-07-26, release date: 2007-04-17, Last modification date: 2024-05-29) |
| Primary citation | Locker, N.,Easton, L.E.,Lukavsky, P.J. HCV and CSFV IRES domain II mediate eIF2 release during 80S ribosome assembly. Embo J., 26:795-805, 2007 Cited by PubMed Abstract: 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. PubMed: 17255934DOI: 10.1038/sj.emboj.7601549 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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