4z4s: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='4z4s' size='340' side='right'caption='[[4z4s]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='4z4s' size='340' side='right'caption='[[4z4s]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4z4s]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4z4s]] 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=4Z4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z4S FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | </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=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4z4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z4s OCA], [https://pdbe.org/4z4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z4s RCSB], [https://www.ebi.ac.uk/pdbsum/4z4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z4s ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5F4T5_9CALI Q5F4T5_9CALI] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 16: | Line 18: | ||
</div> | </div> | ||
<div class="pdbe-citations 4z4s" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4z4s" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 21: | Line 26: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Norovirus | [[Category: Norovirus GII 10]] | ||
[[Category: Hansman | [[Category: Hansman GS]] | ||
[[Category: Koromyslova | [[Category: Koromyslova AD]] | ||
[[Category: Leuthold | [[Category: Leuthold MM]] | ||
Revision as of 10:39, 10 May 2023
Crystal structure of GII.10 P domain in complex with 150mM fucoseCrystal structure of GII.10 P domain in complex with 150mM fucose
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
|
| ||||||||||||||||