4z4u: Difference between revisions
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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=4z4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z4u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4z4u RCSB], [http://www.ebi.ac.uk/pdbsum/4z4u 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=4z4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z4u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4z4u RCSB], [http://www.ebi.ac.uk/pdbsum/4z4u PDBsum]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Human 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<ref>PMID:25980740</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 09:53, 3 June 2015
Crystal structure of GII.10 P domain in complex with 37.5mM fucoseCrystal structure of GII.10 P domain in complex with 37.5mM fucose
Structural highlights
Publication 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. References
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