6out
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Asymmetric focused reconstruction of human norovirus GI.1 Norwalk strain VLP asymmetric unit in T=3 symmetry== | |
+ | <StructureSection load='6out' size='340' side='right'caption='[[6out]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6out]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OUT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OUT FirstGlance]. <br> | ||
+ | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6otf|6otf]]</td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6out FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6out OCA], [http://pdbe.org/6out PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6out RCSB], [http://www.ebi.ac.uk/pdbsum/6out PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6out ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/CAPSD_NVN68 CAPSD_NVN68]] Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells by binding histo-blood group antigens present on gastroduodenal epithelial cells.<ref>PMID:16840313</ref> Soluble capsid protein may play a role in viral immunoevasion.<ref>PMID:16840313</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Noroviruses are a leading cause of foodborne illnesses worldwide. Although GII.4 strains have been responsible for most norovirus outbreaks, the assembled virus shell structures have been available in detail for only a single strain (GI.1). We present high-resolution (2.6- to 4.1-A) cryoelectron microscopy (cryo-EM) structures of GII.4, GII.2, GI.7, and GI.1 human norovirus outbreak strain virus-like particles (VLPs). Although norovirus VLPs have been thought to exist in a single-sized assembly, our structures reveal polymorphism between and within genogroups, with small, medium, and large particle sizes observed. Using asymmetric reconstruction, we were able to resolve a Zn(2+) metal ion adjacent to the coreceptor binding site, which affected the structural stability of the shell. Our structures serve as valuable templates for facilitating vaccine formulations. | ||
- | + | High-resolution cryo-EM structures of outbreak strain human norovirus shells reveal size variations.,Jung J, Grant T, Thomas DR, Diehnelt CW, Grigorieff N, Joshua-Tor L Proc Natl Acad Sci U S A. 2019 Jun 10. pii: 1903562116. doi:, 10.1073/pnas.1903562116. PMID:31182604<ref>PMID:31182604</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 6out" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Diehnelt, C W]] | ||
+ | [[Category: Grant, T]] | ||
+ | [[Category: Grigorieff, N]] | ||
+ | [[Category: Joshua-Tor, L]] | ||
+ | [[Category: Jung, J]] | ||
+ | [[Category: Thomas, D R]] | ||
+ | [[Category: Caliciviridae]] | ||
+ | [[Category: Gi 1]] | ||
+ | [[Category: Norovirus]] | ||
+ | [[Category: Norwalk]] | ||
+ | [[Category: Virus like particle]] |
Revision as of 07:00, 26 June 2019
Asymmetric focused reconstruction of human norovirus GI.1 Norwalk strain VLP asymmetric unit in T=3 symmetry
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