4yg6

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'''Unreleased structure'''
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==Structural basis of glycan recognition in neonate-specific rotaviruses==
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<StructureSection load='4yg6' size='340' side='right' caption='[[4yg6]], [[Resolution|resolution]] 1.46&Aring;' scene=''>
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The entry 4yg6 is ON HOLD until Paper Publication
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4yg6]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YG6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YG6 FirstGlance]. <br>
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Authors: Hu, L., Prasad, B.V.V.
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yg3|4yg3]], [[4ye2|4ye2]], [[4yfw|4yfw]], [[4yfz|4yfz]], [[4yg0|4yg0]]</td></tr>
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Description: Structural basis of glycan recognition in neonate-specific rotaviruses
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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=4yg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yg6 OCA], [http://pdbe.org/4yg6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yg6 RCSB], [http://www.ebi.ac.uk/pdbsum/4yg6 PDBsum]</span></td></tr>
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[[Category: Unreleased Structures]]
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/VP4_ROTBB VP4_ROTBB]] 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. Rotavirus entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. According to the considered strain, VP4 seems to essentially target sialic acid and/or the integrin heterodimer ITGA2/ITGB1 (By similarity). 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 (By similarity). 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 (By similarity).
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__TOC__
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</StructureSection>
[[Category: Hu, L]]
[[Category: Hu, L]]
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[[Category: Prasad, B.V.V]]
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[[Category: Prasad, B V.V]]
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[[Category: Glycan]]
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[[Category: Rotavirus]]
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[[Category: Structural biology]]
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[[Category: Viral protein]]

Revision as of 14:41, 30 September 2015

Structural basis of glycan recognition in neonate-specific rotaviruses

4yg6, resolution 1.46Å

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