2ztn

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Current revision (08:38, 7 February 2024) (edit) (undo)
 
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<StructureSection load='2ztn' size='340' side='right'caption='[[2ztn]], [[Resolution|resolution]] 3.56&Aring;' scene=''>
<StructureSection load='2ztn' size='340' side='right'caption='[[2ztn]], [[Resolution|resolution]] 3.56&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2ztn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hev Hev]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZTN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2ztn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Orthohepevirus_A Orthohepevirus A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZTN FirstGlance]. <br>
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</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=2ztn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ztn OCA], [https://pdbe.org/2ztn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ztn RCSB], [https://www.ebi.ac.uk/pdbsum/2ztn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ztn ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.56&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ztn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ztn OCA], [https://pdbe.org/2ztn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ztn RCSB], [https://www.ebi.ac.uk/pdbsum/2ztn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ztn ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[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]
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Hepatitis E virus (HEV) is a causative agent of acute hepatitis. The crystal structure of HEV-like particles (HEV-LP) consisting of capsid protein was determined at 3.5-A resolution. The capsid protein exhibited a quite different folding at the protruding and middle domains from the members of the families of Caliciviridae and Tombusviridae, while the shell domain shared the common folding. Tyr-288 at the 5-fold axis plays key roles in the assembly of HEV-LP, and aromatic amino acid residues are well conserved among the structurally related viruses. Mutational analyses indicated that the protruding domain is involved in the binding to the cells susceptive to HEV infection and has some neutralization epitopes. These structural and biological findings are important for understanding the molecular mechanisms of assembly and entry of HEV and also provide clues in the development of preventive and prophylactic measures for hepatitis E.
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Biological and immunological characteristics of hepatitis E virus-like particles based on the crystal structure.,Yamashita T, Mori Y, Miyazaki N, Cheng RH, Yoshimura M, Unno H, Shima R, Moriishi K, Tsukihara T, Li TC, Takeda N, Miyamura T, Matsuura Y Proc Natl Acad Sci U S A. 2009 Aug 4;106(31):12986-91. Epub 2009 Jul 20. PMID:19620712<ref>PMID:19620712</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2ztn" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Hev]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Li, T C]]
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[[Category: Orthohepevirus A]]
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[[Category: Matsuura, Y]]
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[[Category: Li TC]]
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[[Category: Mori, Y]]
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[[Category: Matsuura Y]]
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[[Category: Takeda, N]]
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[[Category: Mori Y]]
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[[Category: Unno, H]]
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[[Category: Takeda N]]
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[[Category: Yamashita, T]]
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[[Category: Unno H]]
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[[Category: Virus]]
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[[Category: Yamashita T]]

Current revision

Hepatitis E virus ORF2 (Genotype 3)

PDB ID 2ztn

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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