2l1f
From Proteopedia
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<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> | <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> | ||
</table> | </table> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == 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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2l1f" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Structure of a conserved retroviral RNA packaging element by NMR spectroscopy and cryo-electron tomography
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