3tb0

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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=3tb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tb0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tb0 RCSB], [http://www.ebi.ac.uk/pdbsum/3tb0 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=3tb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tb0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tb0 RCSB], [http://www.ebi.ac.uk/pdbsum/3tb0 PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/VP4_ROTRH VP4_ROTRH]] Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. It is subsequently lost, together with VP7, following virus entry into the host cell. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. In sialic acid-dependent and/or integrin-dependent strains, VP4 seems to essentially target sialic acid and/or the integrin heterodimer ITGA2/ITGB1.<ref>PMID:20375171</ref> Outer capsid protein VP5*: forms the spike "foot" and "body". Acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment.<ref>PMID:20375171</ref> VP8* forms the head of the spikes. It is the viral hemagglutinin and an important target of neutralizing antibodies. In sialic acid-dependent strains, VP8* binds to host cell sialic acid, most probably a ganglioside, providing the initial contact.<ref>PMID:20375171</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 06:44, 24 December 2014

Crystal structure of Rhesus Rotavirus VP8* in complex with N-Glycolylneuraminic acid

3tb0, resolution 2.00Å

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