2.50
Hdl Handle:
http://hdl.handle.net/10033/561176
Title:
Cryo-EM structure of Hepatitis C virus IRES bound to the human ribosome at 3.9-Å resolution.
Authors:
Quade, Nick; Boehringer, Daniel; Leibundgut, Marc; van den Heuvel, Joop ( 0000-0001-5085-4010 ) ; Ban, Nenad
Abstract:
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.
Affiliation:
Helmholtz Centre for Infection Research, Inhoffenstraße 7, 38124 Braunschweig, Germany.
Citation:
Cryo-EM structure of Hepatitis C virus IRES bound to the human ribosome at 3.9-Å resolution. 2015, 6:7646 Nat Commun
Journal:
Nature communications
Issue Date:
2015
URI:
http://hdl.handle.net/10033/561176
DOI:
10.1038/ncomms8646
PubMed ID:
26155016
Type:
Article
Language:
en
ISSN:
2041-1723
Appears in Collections:
publications of the research group recombinant protein expression (RPEX)

Full metadata record

DC FieldValue Language
dc.contributor.authorQuade, Nicken
dc.contributor.authorBoehringer, Danielen
dc.contributor.authorLeibundgut, Marcen
dc.contributor.authorvan den Heuvel, Joopen
dc.contributor.authorBan, Nenaden
dc.date.accessioned2015-07-28T10:41:32Zen
dc.date.available2015-07-28T10:41:32Zen
dc.date.issued2015en
dc.identifier.citationCryo-EM structure of Hepatitis C virus IRES bound to the human ribosome at 3.9-Å resolution. 2015, 6:7646 Nat Communen
dc.identifier.issn2041-1723en
dc.identifier.pmid26155016en
dc.identifier.doi10.1038/ncomms8646en
dc.identifier.urihttp://hdl.handle.net/10033/561176en
dc.description.abstractHepatitis 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.en
dc.language.isoenen
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/250071en
dc.rights.uriopenAccess*
dc.titleCryo-EM structure of Hepatitis C virus IRES bound to the human ribosome at 3.9-Å resolution.en
dc.typeArticleen
dc.contributor.departmentHelmholtz Centre for Infection Research, Inhoffenstraße 7, 38124 Braunschweig, Germany.en
dc.identifier.journalNature communicationsen

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