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| | <StructureSection load='4rpd' size='340' side='right'caption='[[4rpd]], [[Resolution|resolution]] 1.51Å' scene=''> | | <StructureSection load='4rpd' size='340' side='right'caption='[[4rpd]], [[Resolution|resolution]] 1.51Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4rpd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Norwalk_calicivirus Norwalk calicivirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RPD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RPD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4rpd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Norwalk_virus Norwalk virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RPD FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ORF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11983 Norwalk calicivirus])</td></tr> | + | </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=4rpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rpd OCA], [https://pdbe.org/4rpd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rpd RCSB], [https://www.ebi.ac.uk/pdbsum/4rpd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rpd 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=4rpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rpd OCA], [http://pdbe.org/4rpd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rpd RCSB], [http://www.ebi.ac.uk/pdbsum/4rpd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rpd ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q20K66_9CALI Q20K66_9CALI] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4rpd" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4rpd" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Norwalk calicivirus]] | + | [[Category: Norwalk virus]] |
| - | [[Category: Hansman, G S]] | + | [[Category: Hansman GS]] |
| - | [[Category: Singh, B K]] | + | [[Category: Singh BK]] |
| - | [[Category: Hbga]]
| + | |
| - | [[Category: Protruding domain]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| - | [[Category: Virus binding]]
| + | |
| - | [[Category: Virus surface]]
| + | |
| Structural highlights
Function
Q20K66_9CALI
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.
See Also
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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