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| | <StructureSection load='4rpb' size='340' side='right'caption='[[4rpb]], [[Resolution|resolution]] 1.61Å' scene=''> | | <StructureSection load='4rpb' size='340' side='right'caption='[[4rpb]], [[Resolution|resolution]] 1.61Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4rpb]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Norovirus_hu/gii.2/kl109/1978/mys Norovirus hu/gii.2/kl109/1978/mys]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RPB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RPB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4rpb]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RPB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RPB 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></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></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1260940 Norovirus Hu/GII.2/KL109/1978/MYS])</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=4rpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rpb OCA], [https://pdbe.org/4rpb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rpb RCSB], [https://www.ebi.ac.uk/pdbsum/4rpb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rpb ProSAT]</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=4rpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rpb OCA], [http://pdbe.org/4rpb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rpb RCSB], [http://www.ebi.ac.uk/pdbsum/4rpb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rpb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Norovirus hu/gii 2/kl109/1978/mys]] | |
| | [[Category: Hansman, G S]] | | [[Category: Hansman, G S]] |
| | [[Category: Singh, B K]] | | [[Category: Singh, B K]] |
| Structural highlights
Publication Abstract from PubMed
Human norovirus interacts with the polymorphic human histo-blood group antigens (HBGAs), and this interaction is thought to be important for infection. The genogroup II genotype 4 (GII.4) noroviruses are the dominant cluster, evolve every other year, and are thought to modify their binding interactions with different HBGA types. Most human noroviruses bind HBGAs, while some strains were found to have minimal or no HBGA interactions. Here, we explain some possible structural constraints for several noroviruses that were found to bind poorly to HBGAs by using X-ray crystallography. We showed that one aspartic acid was flexible or positioned away from the fucose moiety of the HBGAs and this likely hindered binding, although other fucose-interacting residues were perfectly oriented. Interestingly, a neighboring loop also appeared to influence the loop hosting the aspartic acid. These new findings might explain why some human noroviruses bound HBGAs poorly, although further studies are required.
Structural Constraints on Human Norovirus Binding to Histo-Blood Group Antigens.,Singh BK, Leuthold MM, Hansman GS mSphere. 2016 Mar 30;1(2). pii: e00049-16. doi: 10.1128/mSphere.00049-16., eCollection 2016 Mar-Apr. PMID:27303720[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Singh BK, Leuthold MM, Hansman GS. Structural Constraints on Human Norovirus Binding to Histo-Blood Group Antigens. mSphere. 2016 Mar 30;1(2). pii: e00049-16. doi: 10.1128/mSphere.00049-16., eCollection 2016 Mar-Apr. PMID:27303720 doi:http://dx.doi.org/10.1128/mSphere.00049-16
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