6h9y: Difference between revisions

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'''Unreleased structure'''


The entry 6h9y is ON HOLD  until Paper Publication
==Unraveling the role of the secretor antigen in human rotavirus attachment to histo-blood group antigens==
 
<StructureSection load='6h9y' size='340' side='right'caption='[[6h9y]], [[Resolution|resolution]] 1.31&Aring;' scene=''>
Authors: Ciges-Tomas, J.R., Gozalbo-Rovira, R., Vila-Vicent, S., Buesa, J., Santiso-Bellon, C., Monedero, V., Yebra, M.J., Rodriguez-Diaz, J., Marina, A.
== Structural highlights ==
 
<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>
Description: Molecular bases of histo-blood group antigen recognition by the most common human rotavirus
</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>
[[Category: Unreleased Structures]]
<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>
== 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]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Buesa, J]]
[[Category: Ciges-Tomas, J R]]
[[Category: Gozalbo-Rovira, R]]
[[Category: Marina, A]]
[[Category: Monedero, V]]
[[Category: Monedero, V]]
[[Category: Ciges-Tomas, J.R]]
[[Category: Buesa, J]]
[[Category: Rodriguez-Diaz, J]]
[[Category: Rodriguez-Diaz, J]]
[[Category: Santiso-Bellon, C]]
[[Category: Santiso-Bellon, C]]
[[Category: Yebra, M.J]]
[[Category: Vila-Vicent, S]]
[[Category: Vila-Vicent, S]]
[[Category: Marina, A]]
[[Category: Yebra, M J]]
[[Category: Gozalbo-Rovira, R]]
[[Category: Histo-blood group antigen rotavirus]]
[[Category: Viral protein]]

Revision as of 05:33, 12 June 2019

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

6h9y, resolution 1.31Å

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