8op1
From Proteopedia
(Difference between revisions)
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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=8op1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8op1 OCA], [https://pdbe.org/8op1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8op1 RCSB], [https://www.ebi.ac.uk/pdbsum/8op1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8op1 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=8op1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8op1 OCA], [https://pdbe.org/8op1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8op1 RCSB], [https://www.ebi.ac.uk/pdbsum/8op1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8op1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
- | == Function == | ||
- | [https://www.uniprot.org/uniprot/C3UPA9_9MONO C3UPA9_9MONO] Encapsidates the viral RNA genome by forming a left-handed helical nucleocapsid that protects the RNA from nucleases. RNA replication depends on the availability of soluble nucleoprotein. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication.[RuleBase:RU363106] | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Human Respiratory Syncytial Virus (HRSV) is a prevalent cause of severe respiratory infections in children and the elderly. The helical HRSV nucleocapsid is a template for the viral RNA synthesis and a scaffold for the virion assembly. This cryo-electron microscopy analysis reveals the non-canonical arrangement of the HRSV nucleocapsid helix, composed of 16 nucleoproteins per asymmetric unit, and the resulting systematic variations in the RNA accessibility. We demonstrate that this unique helical symmetry originates from longitudinal interactions by the C-terminal arm of the HRSV nucleoprotein. We explore the polymorphism of the nucleocapsid-like assemblies, report five structures of the full-length particles and two alternative arrangements formed by a C-terminally truncated nucleoprotein mutant, and demonstrate the functional importance of the identified longitudinal interfaces. We put all these findings in the context of the HRSV RNA synthesis machinery and delineate the structural basis for its further investigation. | ||
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- | Structural landscape of the respiratory syncytial virus nucleocapsids.,Gonnin L, Desfosses A, Bacia-Verloop M, Chevret D, Galloux M, Eleouet JF, Gutsche I Nat Commun. 2023 Sep 15;14(1):5732. doi: 10.1038/s41467-023-41439-8. PMID:37714861<ref>PMID:37714861</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 8op1" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Current revision
Subsection of a helical nucleocapsid of the Respiratory Syncytial Virus
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