2il9

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(New page: 200px<br /><applet load="2il9" size="350" color="white" frame="true" align="right" spinBox="true" caption="2il9, resolution 3.100&Aring;" /> '''Crystal Structure o...)
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==Overview==
==Overview==
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Canonical cap-dependent translation initiation requires a large number of, protein factors that act in a stepwise assembly process. In contrast, internal ribosomal entry sites (IRESs) are cis-acting RNAs that in some, cases completely supplant these factors by recruiting and activating the, ribosome using a single structured RNA. Here we present the crystal, structures of the ribosome-binding domain from a Dicistroviridae, intergenic region IRES at 3.1 angstrom resolution, providing a view of the, prefolded architecture of an all-RNA translation initiation apparatus., Docking of the structure into cryo-electron microscopy reconstructions of, an IRES-ribosome complex suggests a model for ribosome manipulation by a, dynamic IRES RNA.
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Canonical cap-dependent translation initiation requires a large number of protein factors that act in a stepwise assembly process. In contrast, internal ribosomal entry sites (IRESs) are cis-acting RNAs that in some cases completely supplant these factors by recruiting and activating the ribosome using a single structured RNA. Here we present the crystal structures of the ribosome-binding domain from a Dicistroviridae intergenic region IRES at 3.1 angstrom resolution, providing a view of the prefolded architecture of an all-RNA translation initiation apparatus. Docking of the structure into cryo-electron microscopy reconstructions of an IRES-ribosome complex suggests a model for ribosome manipulation by a dynamic IRES RNA.
==About this Structure==
==About this Structure==
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Structural basis for ribosome recruitment and manipulation by a viral IRES RNA., Pfingsten JS, Costantino DA, Kieft JS, Science. 2006 Dec 1;314(5804):1450-4. Epub 2006 Nov 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17124290 17124290]
Structural basis for ribosome recruitment and manipulation by a viral IRES RNA., Pfingsten JS, Costantino DA, Kieft JS, Science. 2006 Dec 1;314(5804):1450-4. Epub 2006 Nov 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17124290 17124290]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Costantino, D.A.]]
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[[Category: Costantino, D A.]]
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[[Category: Kieft, J.S.]]
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[[Category: Kieft, J S.]]
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[[Category: Pfingsten, J.S.]]
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[[Category: Pfingsten, J S.]]
[[Category: rna; ires; ribosomal binding domain; psiv; under wound helix; double-nested pseudoknot]]
[[Category: rna; ires; ribosomal binding domain; psiv; under wound helix; double-nested pseudoknot]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:42:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:53:44 2008''

Revision as of 15:53, 21 February 2008


2il9, resolution 3.100Å

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Crystal Structure of Plautia Stali Intestine Virus Intergenic Region Internal Ribosome Entry Site Ribosomal Binding Domain RNA at 3.1 Angstroms

Overview

Canonical cap-dependent translation initiation requires a large number of protein factors that act in a stepwise assembly process. In contrast, internal ribosomal entry sites (IRESs) are cis-acting RNAs that in some cases completely supplant these factors by recruiting and activating the ribosome using a single structured RNA. Here we present the crystal structures of the ribosome-binding domain from a Dicistroviridae intergenic region IRES at 3.1 angstrom resolution, providing a view of the prefolded architecture of an all-RNA translation initiation apparatus. Docking of the structure into cryo-electron microscopy reconstructions of an IRES-ribosome complex suggests a model for ribosome manipulation by a dynamic IRES RNA.

About this Structure

2IL9 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

Reference

Structural basis for ribosome recruitment and manipulation by a viral IRES RNA., Pfingsten JS, Costantino DA, Kieft JS, Science. 2006 Dec 1;314(5804):1450-4. Epub 2006 Nov 23. PMID:17124290

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