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PDBsum entry 5a2q
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Contents |
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216 a.a.
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213 a.a.
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218 a.a.
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225 a.a.
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262 a.a.
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189 a.a.
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230 a.a.
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186 a.a.
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205 a.a.
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180 a.a.
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95 a.a.
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151 a.a.
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123 a.a.
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149 a.a.
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135 a.a.
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120 a.a.
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139 a.a.
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132 a.a.
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143 a.a.
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145 a.a.
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101 a.a.
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82 a.a.
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129 a.a.
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141 a.a.
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124 a.a.
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72 a.a.
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101 a.a.
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82 a.a.
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61 a.a.
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55 a.a.
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56 a.a.
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72 a.a.
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314 a.a.
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24 a.a.
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13 a.a.
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62 a.a.
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References listed in PDB file
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Key reference
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Title
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Cryo-Em structure of hepatitis c virus ires bound to the human ribosome at 3.9-Å resolution.
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Authors
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N.Quade,
D.Boehringer,
M.Leibundgut,
J.Van den heuvel,
N.Ban.
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Ref.
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Nat Commun, 2015,
6,
7646.
[DOI no: ]
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PubMed id
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Abstract
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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.
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