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2ms0
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| - | ''' | + | ==Solution NMR structure pf tRNApro:MLV-Nucleocapsid (1:2) Complex== |
| + | <StructureSection load='2ms0' size='340' side='right' caption='[[2ms0]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2ms0]] is a 3 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MS0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MS0 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mqt|2mqt]], [[2mqv|2mqv]], [[2ms1|2ms1]]</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=2ms0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ms0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ms0 RCSB], [http://www.ebi.ac.uk/pdbsum/2ms0 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | To prime reverse transcription, retroviruses require annealing of a transfer RNA molecule to the U5 primer binding site (U5-PBS) region of the viral genome. The residues essential for primer annealing are initially locked in intramolecular interactions; hence, annealing requires the chaperone activity of the retroviral nucleocapsid (NC) protein to facilitate structural rearrangements. Here we show that, unlike classical chaperones, the Moloney murine leukaemia virus NC uses a unique mechanism for remodelling: it specifically targets multiple structured regions in both the U5-PBS and tRNAPro primer that otherwise sequester residues necessary for annealing. This high-specificity and high-affinity binding by NC consequently liberates these sequestered residues-which are exactly complementary-for intermolecular interactions. Furthermore, NC utilizes a step-wise, entropy-driven mechanism to trigger both residue-specific destabilization and residue-specific release. Our structures of NC bound to U5-PBS and tRNAPro reveal the structure-based mechanism for retroviral primer annealing and provide insights as to how ATP-independent chaperones can target specific RNAs amidst the cellular milieu of non-target RNAs. | ||
| - | + | A structure-based mechanism for tRNA and retroviral RNA remodelling during primer annealing.,Miller SB, Yildiz FZ, Lo JA, Wang B, D'Souza VM Nature. 2014 Sep 7. doi: 10.1038/nature13709. PMID:25209668<ref>PMID:25209668</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Souza, V D.]] | ||
| + | [[Category: Yildiz, Z.]] | ||
| + | [[Category: Nucleocapsid chaperone]] | ||
| + | [[Category: Primer binding site]] | ||
| + | [[Category: Retroviral primer annealing]] | ||
| + | [[Category: Viral protein-rna complex]] | ||
Revision as of 05:54, 8 October 2014
Solution NMR structure pf tRNApro:MLV-Nucleocapsid (1:2) Complex
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