9fns
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of the P domain of the Hepatitis E Virus ORF2 protein in complex with Fab ES1.327== | |
| - | + | <StructureSection load='9fns' size='340' side='right'caption='[[9fns]], [[Resolution|resolution]] 3.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[9fns]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Hepeviridae Hepeviridae] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9FNS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9FNS 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]] 3.5Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=9fns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9fns OCA], [https://pdbe.org/9fns PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9fns RCSB], [https://www.ebi.ac.uk/pdbsum/9fns PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9fns ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CAPSD_HEVUS CAPSD_HEVUS] Plays a role in the inhibition of host antibody-mediated neutralization without blocking viral cell entry.<ref>PMID:29669922</ref> Forms an icosahedral capsid with a T=1 symmetry and a 34 nm diameter. The capsid is composed of 60 copies linked to each other. Binds to the 5' end of the genomic RNA to mediate genome encapsidation (By similarity). Binds to heparin surface proteoglycans (HSPGs) to mediate viral entry. Additionally, the interactions with host ASGR1 and ASGR2 facilitate viral infection of hepatocytes (By similarity). Inhibits IFN production by blocking host TBK1-induced IRF3 phosphorylation (By similarity). The nuclear form probably modulates host gene expression (By similarity).[UniProtKB:P29326][UniProtKB:P33426][UniProtKB:Q81871] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Hepeviridae]] | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Baquero E]] | ||
| + | [[Category: Molinos L]] | ||
| + | [[Category: Mouquet H]] | ||
Current revision
Cryo-EM structure of the P domain of the Hepatitis E Virus ORF2 protein in complex with Fab ES1.327
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