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6h9y

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Current revision (06:47, 3 July 2019) (edit) (undo)
 
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<StructureSection load='6h9y' size='340' side='right'caption='[[6h9y]], [[Resolution|resolution]] 1.31&Aring;' scene=''>
<StructureSection load='6h9y' size='340' side='right'caption='[[6h9y]], [[Resolution|resolution]] 1.31&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6h9y]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H9Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H9Y FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6h9y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_group_a_rotavirus Human group a rotavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H9Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H9Y FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VP4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10941 Human group A rotavirus])</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=6h9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h9y OCA], [http://pdbe.org/6h9y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h9y RCSB], [http://www.ebi.ac.uk/pdbsum/6h9y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h9y ProSAT]</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=6h9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h9y OCA], [http://pdbe.org/6h9y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h9y RCSB], [http://www.ebi.ac.uk/pdbsum/6h9y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h9y ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/A0A2K9UWM4_9REOV A0A2K9UWM4_9REOV]] Outer capsid protein VP5*: Forms the spike "foot" and "body" and acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. During entry, the part of VP5* that protrudes from the virus folds back on itself and reorganizes from a local dimer to a trimer. This reorganization may be linked to membrane penetration by exposing VP5* hydrophobic region. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment.[SAAS:SAAS01043052]
[[http://www.uniprot.org/uniprot/A0A2K9UWM4_9REOV A0A2K9UWM4_9REOV]] Outer capsid protein VP5*: Forms the spike "foot" and "body" and acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. During entry, the part of VP5* that protrudes from the virus folds back on itself and reorganizes from a local dimer to a trimer. This reorganization may be linked to membrane penetration by exposing VP5* hydrophobic region. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment.[SAAS:SAAS01043052]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Rotavirus is the leading agent causing acute gastroenteritis in young children, with the P[8] genotype accounting for more than 80% of infections in humans. The molecular bases for binding of the VP8* domain from P[8] VP4 spike protein to its cellular receptor, the secretory H type-1 antigen (Fuc-alpha1,2-Gal-beta1,3-GlcNAc; H1), and to its precursor lacto-N-biose (Gal-beta1,3-GlcNAc; LNB) have been determined. The resolution of P[8] VP8* crystal structures in complex with H1 antigen and LNB and site-directed mutagenesis experiments revealed that both glycans bind to the P[8] VP8* protein through a binding pocket shared with other members of the P[II] genogroup (i.e.: P[4], P[6] and P[19]). Our results show that the L-fucose moiety from H1 only displays indirect contacts with P[8] VP8*. However, the induced conformational changes in the LNB moiety increase the ligand affinity by two-fold, as measured by surface plasmon resonance (SPR), providing a molecular explanation for the different susceptibility to rotavirus infection between secretor and non-secretor individuals. The unexpected interaction of P[8] VP8* with LNB, a building block of type-1 human milk oligosaccharides, resulted in inhibition of rotavirus infection, highlighting the role and possible application of this disaccharide as an antiviral. While key amino acids in the H1/LNB binding pocket were highly conserved in members of the P[II] genogroup, differences were found in ligand affinities among distinct P[8] genetic lineages. The variation in affinities were explained by subtle structural differences induced by amino acid changes in the vicinity of the binding pocket, providing a fine-tuning mechanism for glycan binding in P[8] rotavirus.
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Unraveling the role of the secretor antigen in human rotavirus attachment to histo-blood group antigens.,Gozalbo-Rovira R, Ciges-Tomas JR, Vila-Vicent S, Buesa J, Santiso-Bellon C, Monedero V, Yebra MJ, Marina A, Rodriguez-Diaz J PLoS Pathog. 2019 Jun 21;15(6):e1007865. doi: 10.1371/journal.ppat.1007865. PMID:31226167<ref>PMID:31226167</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 6h9y" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human group a rotavirus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Buesa, J]]
[[Category: Buesa, J]]

Current revision

Unraveling the role of the secretor antigen in human rotavirus attachment to histo-blood group antigens

PDB ID 6h9y

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