6s6l
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of murine norovirus (MNV-1)== | |
| + | <StructureSection load='6s6l' size='340' side='right'caption='[[6s6l]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S6L 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]] 3.1Å</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=6s6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s6l OCA], [https://pdbe.org/6s6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s6l RCSB], [https://www.ebi.ac.uk/pdbsum/6s6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s6l ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Icosahedral viral capsids must undergo conformational rearrangements to coordinate essential processes during the viral life cycle. Capturing such conformational flexibility has been technically challenging yet could be key for developing rational therapeutic agents to combat infections. Noroviruses are nonenveloped, icosahedral viruses of global importance to human health. They are a common cause of acute gastroenteritis, yet no vaccines or specific antiviral agents are available. Here, we use genetics and cryo-electron microscopy (cryo-EM) to study the high-resolution solution structures of murine norovirus as a model for human viruses. By comparing our 3 structures (at 2.9- to 3.1-A resolution), we show that whilst there is little change to the shell domain of the capsid, the radiating protruding domains are flexible, adopting distinct states both independently and synchronously. In doing so, the capsids sample a range of conformational space, with implications for maintaining virion stability and infectivity. | ||
| - | + | Dynamics in the murine norovirus capsid revealed by high-resolution cryo-EM.,Snowden JS, Hurdiss DL, Adeyemi OO, Ranson NA, Herod MR, Stonehouse NJ PLoS Biol. 2020 Mar 31;18(3):e3000649. doi: 10.1371/journal.pbio.3000649., eCollection 2020 Mar. PMID:32231352<ref>PMID:32231352</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6s6l" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Adeyemi OO]] | ||
| + | [[Category: Herod MR]] | ||
| + | [[Category: Hurdiss DL]] | ||
| + | [[Category: Ranson NA]] | ||
| + | [[Category: Snowden JS]] | ||
| + | [[Category: Stonehouse NJ]] | ||
Current revision
Cryo-EM structure of murine norovirus (MNV-1)
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