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PDBsum entry 3pyv
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271 a.a.
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204 a.a.
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202 a.a.
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181 a.a.
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159 a.a.
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145 a.a.
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32 a.a.
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137 a.a.
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122 a.a.
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146 a.a.
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136 a.a.
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117 a.a.
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98 a.a.
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137 a.a.
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116 a.a.
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101 a.a.
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112 a.a.
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92 a.a.
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100 a.a.
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188 a.a.
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76 a.a.
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88 a.a.
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62 a.a.
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59 a.a.
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30 a.a.
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52 a.a.
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44 a.a.
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48 a.a.
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63 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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Crystal structures of complexes containing domains from two viral internal ribosome entry site (ires) rnas bound to the 70s ribosome.
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Authors
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J.Zhu,
A.Korostelev,
D.A.Costantino,
J.P.Donohue,
H.F.Noller,
J.S.Kieft.
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Ref.
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Proc Natl Acad Sci U S A, 2011,
108,
1839-1844.
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PubMed id
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Abstract
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Internal ribosome entry site (IRES) RNAs are elements of viral or cellular mRNAs
that bypass steps of canonical eukaryotic cap-dependent translation initiation.
Understanding of the structural basis of IRES mechanisms is limited, partially
due to a lack of high-resolution structures of IRES RNAs bound to their cellular
targets. Prompted by the universal phylogenetic conservation of the ribosomal P
site, we solved the crystal structures of proposed P site binding domains from
two intergenic region IRES RNAs bound to bacterial 70S ribosomes. The structures
show that these IRES domains nearly perfectly mimic a tRNA • mRNA interaction.
However, there are clear differences in the global shape and position of this
IRES domain in the intersubunit space compared to those of tRNA, supporting a
mechanism for IRES action that invokes hybrid state mimicry to drive a
noncanonical mode of translocation. These structures suggest how relatively
small structured RNAs can manipulate complex biological machines.
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