7yg7

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Current revision (07:32, 3 July 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7yg7]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Carp_sprivivirus Carp sprivivirus] and [https://en.wikipedia.org/wiki/Trichoplusia_ni Trichoplusia ni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YG7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[7yg7]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Carp_sprivivirus Carp sprivivirus] and [https://en.wikipedia.org/wiki/Trichoplusia_ni Trichoplusia ni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YG7 FirstGlance]. <br>
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</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=7yg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yg7 OCA], [https://pdbe.org/7yg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yg7 RCSB], [https://www.ebi.ac.uk/pdbsum/7yg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yg7 ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.7&#8491;</td></tr>
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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=7yg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yg7 OCA], [https://pdbe.org/7yg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yg7 RCSB], [https://www.ebi.ac.uk/pdbsum/7yg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yg7 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NCAP_SVCV NCAP_SVCV] Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. Nucleocapsid assembly is concommitant with replication, therefore viral replication depends on the intracellular concentration of free N, termed N(0). All replicative products are resistant to nucleases.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Spring viremia of carp virus (SVCV) is a highly pathogenic Vesiculovirus infecting the common carp, yet neither a vaccine nor effective therapies are available to treat spring viremia of carp (SVC). Like all negative-sense viruses, SVCV contains an RNA genome that is encapsidated by the nucleoprotein (N) in the form of a ribonucleoprotein (RNP) complex, which serves as the template for viral replication and transcription. Here, the three-dimensional (3D) structure of SVCV RNP was resolved through cryo-electron microscopy (cryo-EM) at a resolution of 3.7 A. RNP assembly was stabilized by N and C loops; RNA was wrapped in the groove between the N and C lobes with 9 nt nucleotide per protomer. Combined with mutational analysis, our results elucidated the mechanism of RNP formation. The RNA binding groove of SVCV N was used as a target for drug virtual screening, and it was found suramin had a good antiviral effect. This study provided insights into RNP assembly, and anti-SVCV drug screening was performed on the basis of this structure, providing a theoretical basis and efficient drug screening method for the prevention and treatment of SVC. IMPORTANCE Aquaculture accounts for about 70% of global aquatic products, and viral diseases severely harm the development of aquaculture industry. Spring viremia of carp virus (SVCV) is the pathogen causing highly contagious spring viremia of carp (SVC) disease in cyprinids, especially common carp (Cyprinus carpio), yet neither a vaccine nor effective therapies are available to treat this disease. In this study, we have elucidated the mechanism of SVCV ribonucleoprotein complex (RNP) formation by resolving the 3D structure of SVCV RNP and screened antiviral drugs based on the structure. It is found that suramin could competitively bind to the RNA binding groove and has good antiviral effects both in vivo and in vitro. Our study provides a template for rational drug discovery efforts to treat and prevent SVCV infections.
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Structure of the Spring Viraemia of Carp Virus Ribonucleoprotein Complex Reveals Its Assembly Mechanism and Application in Antiviral Drug Screening.,Wang ZX, Liu B, Yang T, Yu D, Zhang C, Zheng L, Xie J, Liu B, Liu M, Peng H, Lai L, Ouyang Q, Ouyang S, Zhang YA J Virol. 2023 Apr 27;97(4):e0182922. doi: 10.1128/jvi.01829-22. Epub 2023 Mar 21. PMID:36943056<ref>PMID:36943056</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7yg7" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Nucleoprotein 3D structures|Nucleoprotein 3D structures]]
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== References ==
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<references/>
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</StructureSection>
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Current revision

Structure of the Spring Viraemia of Carp Virus ribonucleoprotein Complex

PDB ID 7yg7

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