3ggq

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==Dimerization of Hepatitis E Virus Capsid Protein E2s Domain is Essential for Virus-Host Interaction==
==Dimerization of Hepatitis E Virus Capsid Protein E2s Domain is Essential for Virus-Host Interaction==
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<StructureSection load='3ggq' size='340' side='right' caption='[[3ggq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='3ggq' size='340' side='right'caption='[[3ggq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ggq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hepatitis_e_virus_(strain_pakistan) Hepatitis e virus (strain pakistan)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GGQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GGQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ggq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hepatitis_E_virus_(strain_Pakistan) Hepatitis E virus (strain Pakistan)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GGQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GGQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></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]] 2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ORF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=33774 Hepatitis E virus (strain Pakistan)])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr>
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<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=3ggq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ggq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ggq RCSB], [http://www.ebi.ac.uk/pdbsum/3ggq PDBsum]</span></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=3ggq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ggq OCA], [https://pdbe.org/3ggq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ggq RCSB], [https://www.ebi.ac.uk/pdbsum/3ggq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ggq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CAPSD_HEVPA CAPSD_HEVPA]] Major viral capsid protein that encapsidates the viral genome. Binds to the 5' end of the genomic RNA (By similarity).
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[https://www.uniprot.org/uniprot/CAPSD_HEVPA CAPSD_HEVPA] Major viral capsid protein that encapsidates the viral genome. Binds to the 5' end of the genomic RNA (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gg/3ggq_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gg/3ggq_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ggq ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Hepatitis E virus (HEV), a non-enveloped, positive-stranded RNA virus, is transmitted in a faecal-oral manner, and causes acute liver diseases in humans. The HEV capsid is made up of capsomeres consisting of homodimers of a single structural capsid protein forming the virus shell. These dimers are believed to protrude from the viral surface and to interact with host cells to initiate infection. To date, no structural information is available for any of the HEV proteins. Here, we report for the first time the crystal structure of the HEV capsid protein domain E2s, a protruding domain, together with functional studies to illustrate that this domain forms a tight homodimer and that this dimerization is essential for HEV-host interactions. In addition, we also show that the neutralizing antibody recognition site of HEV is located on the E2s domain. Our study will aid in the development of vaccines and, subsequently, specific inhibitors for HEV.
 
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Dimerization of hepatitis E virus capsid protein E2s domain is essential for virus-host interaction.,Li S, Tang X, Seetharaman J, Yang C, Gu Y, Zhang J, Du H, Shih JW, Hew CL, Sivaraman J, Xia N PLoS Pathog. 2009 Aug;5(8):e1000537. Epub 2009 Aug 7. PMID:19662165<ref>PMID:19662165</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>
 
==See Also==
==See Also==
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*[[Virus coat protein|Virus coat protein]]
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Du, H L]]
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[[Category: Large Structures]]
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[[Category: Gu, Y]]
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[[Category: Du HL]]
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[[Category: Hew, C L]]
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[[Category: Gu Y]]
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[[Category: Li, S W]]
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[[Category: Hew CL]]
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[[Category: Seetharaman, J]]
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[[Category: Li SW]]
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[[Category: Shih, J W.K]]
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[[Category: Seetharaman J]]
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[[Category: Sivaraman, J]]
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[[Category: Shih JWK]]
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[[Category: Tang, X H]]
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[[Category: Sivaraman J]]
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[[Category: Xia, N S]]
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[[Category: Tang XH]]
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[[Category: Yang, C Y]]
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[[Category: Xia NS]]
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[[Category: Zhang, J]]
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[[Category: Yang CY]]
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[[Category: Beta barrel]]
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[[Category: Zhang J]]
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[[Category: Capsid protein]]
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[[Category: Rna-binding]]
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[[Category: Viral protein]]
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Current revision

Dimerization of Hepatitis E Virus Capsid Protein E2s Domain is Essential for Virus-Host Interaction

PDB ID 3ggq

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