2mqt

<StructureSection load='2mqt' size='340' side='right'caption='[[2mqt]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[2mqt]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MQT FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2mqv|2mqv]], [[2ms0|2ms0]], [[2ms1|2ms1]]</div></td></tr>

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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2mqt" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Souza, V D]]

[[Category: Yildiz, Z]]

[[Category: Rna]]

[[Category: Ynmg tetraloop]]