2l1f

<StructureSection load='2l1f' size='340' side='right'caption='[[2l1f]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[2l1f]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L1F FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2l1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l1f OCA], [https://pdbe.org/2l1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l1f RCSB], [https://www.ebi.ac.uk/pdbsum/2l1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l1f ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The 5'-untranslated regions of all gammaretroviruses contain a conserved "double-hairpin motif" (Psi(CD)) that is required for genome packaging. Both hairpins (SL-C and SL-D) contain GACG tetraloops that, in isolated RNAs, are capable of forming "kissing" interactions stabilized by two intermolecular G-C base pairs. We have determined the three-dimensional structure of the double hairpin from the Moloney murine leukemia virus ([Psi(CD)](2), 132 nt, 42.8 kDa) using a (2)H-edited NMR-spectroscopy-based approach. This approach enabled the detection of (1)H-(1)H dipolar interactions that were not observed in previous studies of isolated SL-C and SL-D hairpin RNAs using traditional (1)H-(1)H correlated and (1)H-(13)C-edited NMR methods. The hairpins participate in intermolecular cross-kissing interactions (SL-C to SL-D' and SLC' to SL-D) and stack in an end-to-end manner (SL-C to SL-D and SL-C' to SL-D') that gives rise to an elongated overall shape (ca 95 Ax45 Ax25 A). The global structure was confirmed by cryo-electron tomography (cryo-ET), making [Psi(CD)](2) simultaneously the smallest RNA to be structurally characterized to date by cryo-ET and among the largest to be determined by NMR. Our findings suggest that, in addition to promoting dimerization, [Psi(CD)](2) functions as a scaffold that helps initiate virus assembly by exposing a cluster of conserved UCUG elements for binding to the cognate nucleocapsid domains of assembling viral Gag proteins.

Structure of a Conserved Retroviral RNA Packaging Element by NMR Spectroscopy and Cryo-Electron Tomography.,Miyazaki Y, Irobalieva RN, Tolbert B, Smalls-Mantey A, Iyalla K, Loeliger K, D'Souza V, Khant H, Schmid MF, Garcia E, Telesnitsky A, Chiu W, Summers MF J Mol Biol. 2010 Oct 8. PMID:20933521<ref>PMID:20933521</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 2l1f" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Chiu, W]]

[[Category: Garcia, E]]

[[Category: Irobalieva, R N]]

[[Category: Iyalla, K]]

[[Category: Khant, H]]

[[Category: Loeliger, K]]

[[Category: Miyazaki, Y]]

[[Category: Schmid, M]]

[[Category: Smalls-Manty, A]]

[[Category: Souza, V D]]

[[Category: Summers, M F]]

[[Category: Telesnitsky, A]]

[[Category: Tolbert, B]]

[[Category: Rna]]