3sit: Difference between revisions
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<StructureSection load='3sit' size='340' side='right'caption='[[3sit]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='3sit' size='340' side='right'caption='[[3sit]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3sit]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Porcine_rotavirus_(serotype_3_/ | <table><tr><td colspan='2'>[[3sit]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Porcine_rotavirus_(serotype_3_/_strain_CRW-8) Porcine rotavirus (serotype 3 / strain CRW-8)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SIT FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand= | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PRD_900025:3-sialyl-alpha-lactose'>PRD_900025</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3sit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sit OCA], [https://pdbe.org/3sit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sit RCSB], [https://www.ebi.ac.uk/pdbsum/3sit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sit ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3sit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sit OCA], [https://pdbe.org/3sit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sit RCSB], [https://www.ebi.ac.uk/pdbsum/3sit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sit ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/VP4_ROTP3 VP4_ROTP3] 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). | |||
==See Also== | ==See Also== | ||
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Blanchard | [[Category: Blanchard H]] | ||
[[Category: Yu | [[Category: Yu X]] | ||
Latest revision as of 15:57, 14 March 2024
Crystal structure of porcine CRW-8 Rotavirus VP8* in complex with aceramido-GM3Crystal structure of porcine CRW-8 Rotavirus VP8* in complex with aceramido-GM3
Structural highlights
FunctionVP4_ROTP3 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). See Also |
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