2xl1

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[[Image:2xl1.png|left|200px]]
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==STRUCTURAL BASIS OF TRANSLATIONAL STALLING BY HUMAN CYTOMEGALOVIRUS (HCMV) AND FUNGAL ARGININE ATTENUATOR PEPTIDE (AAP)==
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<StructureSection load='2xl1' size='340' side='right' caption='[[2xl1]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2xl1]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XL1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XL1 FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xl1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xl1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xl1 RCSB], [http://www.ebi.ac.uk/pdbsum/2xl1 PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Specific regulatory nascent chains establish direct interactions with the ribosomal tunnel, leading to translational stalling. Despite a wealth of biochemical data, structural insight into the mechanism of translational stalling in eukaryotes is still lacking. Here we use cryo-electron microscopy to visualize eukaryotic ribosomes stalled during the translation of two diverse regulatory peptides: the fungal arginine attenuator peptide (AAP) and the human cytomegalovirus (hCMV) gp48 upstream open reading frame 2 (uORF2). The C terminus of the AAP appears to be compacted adjacent to the peptidyl transferase center (PTC). Both nascent chains interact with ribosomal proteins L4 and L17 at tunnel constriction in a distinct fashion. Significant changes at the PTC were observed: the eukaryotic-specific loop of ribosomal protein L10e establishes direct contact with the CCA end of the peptidyl-tRNA (P-tRNA), which may be critical for silencing of the PTC during translational stalling. Our findings provide direct structural insight into two distinct eukaryotic stalling processes.
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{{STRUCTURE_2xl1| PDB=2xl1 | SCENE= }}
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Structural basis for translational stalling by human cytomegalovirus and fungal arginine attenuator peptide.,Bhushan S, Meyer H, Starosta AL, Becker T, Mielke T, Berninghausen O, Sattler M, Wilson DN, Beckmann R Mol Cell. 2010 Oct 8;40(1):138-46. PMID:20932481<ref>PMID:20932481</ref>
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===STRUCTURAL BASIS OF TRANSLATIONAL STALLING BY HUMAN CYTOMEGALOVIRUS (HCMV) AND FUNGAL ARGININE ATTENUATOR PEPTIDE (AAP)===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_20932481}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2xl1]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XL1 OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:020932481</ref><references group="xtra"/>
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[[Category: Meyer, N H.]]
[[Category: Meyer, N H.]]
[[Category: Sattler, M.]]
[[Category: Sattler, M.]]

Revision as of 13:13, 22 October 2014

STRUCTURAL BASIS OF TRANSLATIONAL STALLING BY HUMAN CYTOMEGALOVIRUS (HCMV) AND FUNGAL ARGININE ATTENUATOR PEPTIDE (AAP)

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