Cryo-EM structure of Hepatitis C virus IRES bound to the human ribosome at 3.9-angstrom resolution
| LEADER | caa a22 4500 | ||
|---|---|---|---|
| 001 | 528785869 | ||
| 005 | 20190713030955.0 | ||
| 007 | cr unu---uuuuu | ||
| 008 | 180924s2015 xx s 000 0 eng | ||
| 024 | 7 | 0 | |a 10.3929/ethz-b-000103868 |2 doi |
| 024 | 7 | 0 | |a 10.1038/ncomms8646 |2 doi |
| 035 | |a (ETHRESEARCH)oai:www.research-collecti.ethz.ch:20.500.11850/103868 | ||
| 245 | 0 | 0 | |a Cryo-EM structure of Hepatitis C virus IRES bound to the human ribosome at 3.9-angstrom resolution |h [Elektronische Daten] |c [Nick Quade, Daniel Boehringer, Marc Leibundgut, Joop Van den Heuvel, Nenad Ban] |
| 246 | 0 | |a Nat Commun | |
| 506 | |a Open access |2 ethresearch | ||
| 520 | 3 | |a Hepatitis C virus (HCV), a widespread human pathogen, is dependent on a highly structured 5′-untranslated region of its mRNA, referred to as internal ribosome entry site (IRES), for the translation of all of its proteins. The HCV IRES initiates translation by directly binding to the small ribosomal subunit (40S), circumventing the need for many eukaryotic translation initiation factors required for mRNA scanning. Here we present the cryo-EM structure of the human 40S ribosomal subunit in complex with the HCV IRES at 3.9 Å resolution, determined by focused refinement of an 80S ribosome-HCV IRES complex. The structure reveals the molecular details of the interactions between the IRES and the 40S, showing that expansion segment 7 (ES7) of the 18S rRNA acts as a central anchor point for the HCV IRES. The structural data rationalizes previous biochemical and genetic evidence regarding the initiation mechanism of the HCV and other related IRESs. | |
| 540 | |a Creative Commons Attribution 4.0 International |u http://creativecommons.org/licenses/by/4.0 |2 ethresearch | ||
| 700 | 1 | |a Quade |D Nick |e joint author | |
| 700 | 1 | |a Boehringer |D Daniel |e joint author | |
| 700 | 1 | |a Leibundgut |D Marc |e joint author | |
| 700 | 1 | |a Van den Heuvel |D Joop |e joint author | |
| 700 | 1 | |a Ban |D Nenad |e joint author | |
| 773 | 0 | |t Nature Communications |d London : Nature Publishing Group |g 6, p. 7646 |x 2041-1723 | |
| 856 | 4 | 0 | |u http://hdl.handle.net/20.500.11850/103868 |q text/html |z WWW-Backlink auf das Repository (Open access) |
| 908 | |D 1 |a Journal Article |2 ethresearch | ||
| 950 | |B ETHRESEARCH |P 856 |E 40 |u http://hdl.handle.net/20.500.11850/103868 |q text/html |z WWW-Backlink auf das Repository (Open access) | ||
| 950 | |B ETHRESEARCH |P 700 |E 1- |a Quade |D Nick |e joint author | ||
| 950 | |B ETHRESEARCH |P 700 |E 1- |a Boehringer |D Daniel |e joint author | ||
| 950 | |B ETHRESEARCH |P 700 |E 1- |a Leibundgut |D Marc |e joint author | ||
| 950 | |B ETHRESEARCH |P 700 |E 1- |a Van den Heuvel |D Joop |e joint author | ||
| 950 | |B ETHRESEARCH |P 700 |E 1- |a Ban |D Nenad |e joint author | ||
| 950 | |B ETHRESEARCH |P 773 |E 0- |t Nature Communications |d London : Nature Publishing Group |g 6, p. 7646 |x 2041-1723 | ||
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 949 | |B ETHRESEARCH |F ETHRESEARCH |b ETHRESEARCH |j Journal Article |c Open access | ||