View source for 7qvx


==Cryo-EM structure of coxsackievirus A6 altered particle==
<StructureSection load='7qvx' size='340' side='right'caption='[[7qvx]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7qvx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Coxsackievirus_A6 Coxsackievirus A6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QVX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QVX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.5&#8491;</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=7qvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qvx OCA], [https://pdbe.org/7qvx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qvx RCSB], [https://www.ebi.ac.uk/pdbsum/7qvx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qvx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6JKS2_9ENTO Q6JKS2_9ENTO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Coxsackievirus A6 (CV-A6) has recently overtaken enterovirus A71 and CV-A16 as the primary causative agent of hand, foot, and mouth disease worldwide. Virions of CV-A6 were not identified in previous structural studies, and it was speculated that the virus is unique among enteroviruses in using altered particles with expanded capsids to infect cells. In contrast, the virions of other enteroviruses are required for infection. Here we used cryo-electron microscopy (cryo-EM) to determine the structures of the CV-A6 virion, altered particle, and empty capsid. We show that the CV-A6 virion has features characteristic of virions of other enteroviruses, including a compact capsid, VP4 attached to the inner capsid surface, and fatty acid-like molecules occupying the hydrophobic pockets in VP1 subunits. Furthermore, we found that in a purified sample of CV-A6, the ratio of infectious units to virions is 1 to 500. Therefore, it is likely that virions of CV-A6 initiate infection, like those of other enteroviruses. Our results provide evidence that future vaccines against CV-A6 should target its virions instead of the antigenically distinct altered particles. Furthermore, the structure of the virion provides the basis for the rational development of capsid-binding inhibitors that block the genome release of CV-A6.

Cryo-electron microscopy and image classification reveal the existence and structure of the coxsackievirus A6 virion.,Buttner CR, Spurny R, Fuzik T, Plevka P Commun Biol. 2022 Sep 2;5(1):898. doi: 10.1038/s42003-022-03863-2. PMID:36056184<ref>PMID:36056184</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7qvx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Coxsackievirus A6]]
[[Category: Large Structures]]
[[Category: Buttner CR]]
[[Category: Fuzik T]]
[[Category: Plevka P]]
[[Category: Spurny R]]