4z4y: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4z4y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Norovirus_GII.10 Norovirus GII.10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z4Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z4Y FirstGlance]. <br> | <table><tr><td colspan='2'>[[4z4y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Norovirus_GII.10 Norovirus GII.10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z4Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z4Y FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.797Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</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=4z4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z4y OCA], [https://pdbe.org/4z4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z4y RCSB], [https://www.ebi.ac.uk/pdbsum/4z4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z4y 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=4z4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z4y OCA], [https://pdbe.org/4z4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z4y RCSB], [https://www.ebi.ac.uk/pdbsum/4z4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z4y ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 13:58, 10 January 2024
Crystal structure of GII.10 P domain in complex with 7.5mM B antigen (trisaccharide)Crystal structure of GII.10 P domain in complex with 7.5mM B antigen (trisaccharide)
Structural highlights
FunctionPublication Abstract from PubMedHuman noroviruses bind histo-blood group antigens (HBGAs) and this interaction is thought to be important for an infection. We identified two additional fucose-binding pockets (termed fucose-3/4 sites) on a genogroup II human (GII.10) norovirus-protruding (P) dimer using X-ray crystallography. Fucose-3/4 sites were located between two previously determined HBGA binding pockets (termed fucose-1/2 sites). We found that four fucose molecules were capable of binding altogether at fucose-1/2/3/4 sites on the P dimer, though the fucose molecules bound in a dose-dependent and step-wise manner. We also showed that HBGA B-trisaccharide molecules bound in a similar way at the fucose-1/2 sites. Interestingly, we discovered that the monomers of the P dimer were asymmetrical in an unliganded state and when a single B-trisaccharide molecule bound, but were symmetrical when two B-trisaccharide molecules bound. We postulate that the symmetrical dimers might favor HBGA binding interactions at fucose-1/2 sites. The sweet quartet: Binding of fucose to the norovirus capsid.,Koromyslova AD, Leuthold MM, Bowler MW, Hansman GS Virology. 2015 May 13;483:203-208. doi: 10.1016/j.virol.2015.04.006. PMID:25980740[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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