2zzq: Difference between revisions
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<StructureSection load='2zzq' size='340' side='right'caption='[[2zzq]], [[Resolution|resolution]] 3.81Å' scene=''> | <StructureSection load='2zzq' size='340' side='right'caption='[[2zzq]], [[Resolution|resolution]] 3.81Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2zzq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2zzq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hepatitis_E_virus_(strain_Myanmar) Hepatitis E virus (strain Myanmar)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZZQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZZQ FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.81Å</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=2zzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zzq OCA], [https://pdbe.org/2zzq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zzq RCSB], [https://www.ebi.ac.uk/pdbsum/2zzq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zzq ProSAT]</span></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=2zzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zzq OCA], [https://pdbe.org/2zzq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zzq RCSB], [https://www.ebi.ac.uk/pdbsum/2zzq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zzq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[https://www.uniprot.org/uniprot/ORF3_HEVBU ORF3_HEVBU | [https://www.uniprot.org/uniprot/CAPSD_HEVBU CAPSD_HEVBU] Plays a role in the inhibition of host antibody-mediated neutralization without blocking viral cell entry.[UniProtKB:Q9YLQ9] 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 (PubMed:14671114, PubMed:15557331). Binds to heparin surface proteoglycans (HSPGs) to mediate viral entry (By similarity). 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:P33426][UniProtKB:Q81871]<ref>PMID:14671114</ref> <ref>PMID:15557331</ref> [https://www.uniprot.org/uniprot/ORF3_HEVBU ORF3_HEVBU] May act as a viral regulatory protein involved in the modulation of mitogenic signaling pathways. May be involved in virion morphogenesis and viral pathogenesis. Expedites the processing and secretion of AMBP from the hepatocyte (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cheng | [[Category: Cheng RH]] | ||
[[Category: Higashiura | [[Category: Higashiura A]] | ||
[[Category: Li | [[Category: Li T-C]] | ||
[[Category: Miyamura | [[Category: Miyamura T]] | ||
[[Category: Miyazaki | [[Category: Miyazaki N]] | ||
[[Category: Nakagawa | [[Category: Nakagawa A]] | ||
[[Category: Takeda | [[Category: Takeda N]] | ||
[[Category: Tsukihara | [[Category: Tsukihara T]] | ||
[[Category: Wang | [[Category: Wang C-Y]] | ||
[[Category: Xing | [[Category: Xing L]] | ||
Latest revision as of 16:59, 13 March 2024
Crystal structure analysis of the HEV capsid protein, PORF2Crystal structure analysis of the HEV capsid protein, PORF2
Structural highlights
FunctionCAPSD_HEVBU Plays a role in the inhibition of host antibody-mediated neutralization without blocking viral cell entry.[UniProtKB:Q9YLQ9] 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 (PubMed:14671114, PubMed:15557331). Binds to heparin surface proteoglycans (HSPGs) to mediate viral entry (By similarity). 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:P33426][UniProtKB:Q81871][1] [2] ORF3_HEVBU May act as a viral regulatory protein involved in the modulation of mitogenic signaling pathways. May be involved in virion morphogenesis and viral pathogenesis. Expedites the processing and secretion of AMBP from the hepatocyte (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
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