3rkc: Difference between revisions
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==Hepatitis E Virus Capsid Protein E2s Domain (genotype IV)== | ==Hepatitis E Virus Capsid Protein E2s Domain (genotype IV)== | ||
<StructureSection load='3rkc' size='340' side='right' caption='[[3rkc]], [[Resolution|resolution]] 1.79Å' scene=''> | <StructureSection load='3rkc' size='340' side='right' caption='[[3rkc]], [[Resolution|resolution]] 1.79Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3rkc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3rkc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Hev Hev]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RKC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RKC FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rkd|3rkd]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rkd|3rkd]]</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=3rkc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rkc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rkc RCSB], [http://www.ebi.ac.uk/pdbsum/3rkc PDBsum]</span></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=3rkc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rkc OCA], [http://pdbe.org/3rkc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rkc RCSB], [http://www.ebi.ac.uk/pdbsum/3rkc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rkc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3rkc" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Hev]] | ||
[[Category: Sivaraman, J]] | [[Category: Sivaraman, J]] | ||
[[Category: Tang, X H]] | [[Category: Tang, X H]] | ||
[[Category: Viral capsid protein]] | [[Category: Viral capsid protein]] | ||
[[Category: Viral protein]] | [[Category: Viral protein]] | ||
Revision as of 17:28, 5 August 2016
Hepatitis E Virus Capsid Protein E2s Domain (genotype IV)Hepatitis E Virus Capsid Protein E2s Domain (genotype IV)
Structural highlights
Publication Abstract from PubMedHepatitis E virus (HEV) causes acute hepatitis in humans, predominantly by contamination of food and water, and is characterized by jaundice and flu-like aches and pains. To date, no vaccines are commercially available to prevent the disease caused by HEV. Previously, we showed that a monoclonal antibody, 8C11, specifically recognizes a neutralizing conformational epitope on HEV genotype I. The antibody 8C11 blocks the virus-like particle from binding to and penetrating the host cell. Here, we report the complex crystal structure of 8C11 Fab with HEV E2s(I) domain at 1.9 A resolution. The 8C11 epitopes on E2s(I) were identified at Asp(496)-Thr(499), Val(510)-Leu(514), and Asn(573)-Arg(578). Mutations and cell-model assays identified Arg(512) as the most crucial residue for 8C11 interaction with and neutralization of HEV. Interestingly, 8C11 specifically neutralizes HEV genotype I, but not the other genotypes. Because HEV type I and IV are the most abundant genotypes, to understand this specificity further we determined the structure of E2s(IV) at 1.79 A resolution and an E2s(IV) complex with 8C11 model was generated. The comparison between the 8C11 complexes with type I and IV revealed the key residues that distinguish these two genotypes. Of particular interest, the residue at amino acid position 497 at the 8C11 epitope region of E2s is distinct among these two genotypes. Swapping this residue from one genotype to another inversed the 8C11 reactivity, demonstrating the essential role played by amino acid 497 in the genotype recognition. These studies may lead to the development of antibody-based drugs for the specific treatment against HEV. Structural basis for the neutralization and genotype specificity of hepatitis E virus.,Tang X, Yang C, Gu Y, Song C, Zhang X, Wang Y, Zhang J, Hew CL, Li S, Xia N, Sivaraman J Proc Natl Acad Sci U S A. 2011 Jun 21;108(25):10266-71. Epub 2011 Jun 3. PMID:21642534[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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