4qv2: 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=4qv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qv2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qv2 RCSB], [http://www.ebi.ac.uk/pdbsum/4qv2 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=4qv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qv2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qv2 RCSB], [http://www.ebi.ac.uk/pdbsum/4qv2 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Norovirus infects different animals, including humans, mice, dogs, and cats. Here, we show an X-ray crystal structure of a feline GIV.2 norovirus capsid-protruding (P) domain to 2.35A resolution. The feline GIV.2 P domain was reminiscent of human norovirus P domains, except for a novel P2 subdomain alpha-helix and an extended P1 subdomain interface loop. These new structural features likely obstructed histo-blood group antigens, which are attachment factors for human norovirus, from binding at the equivalent sites on the feline GIV.2 P domain. Additionally, an ELISA showed that the feline GIV.2 was antigenically distinct from a human GII.10 norovirus. | |||
Structural analysis of a feline norovirus protruding domain.,Singh BK, Glatt S, Ferrer JL, Koromyslova AD, Leuthold MM, Dunder J, Hansman GS Virology. 2015 Jan 1;474:181-5. doi: 10.1016/j.virol.2014.10.028. Epub 2014 Nov, 19. PMID:25463616<ref>PMID:25463616</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||
Revision as of 14:24, 4 March 2015
Unliganded crystal structure of Feline Norovirus P Domain co-crystallized with HBGA A-trisaccharideUnliganded crystal structure of Feline Norovirus P Domain co-crystallized with HBGA A-trisaccharide
Structural highlights
Publication Abstract from PubMedNorovirus infects different animals, including humans, mice, dogs, and cats. Here, we show an X-ray crystal structure of a feline GIV.2 norovirus capsid-protruding (P) domain to 2.35A resolution. The feline GIV.2 P domain was reminiscent of human norovirus P domains, except for a novel P2 subdomain alpha-helix and an extended P1 subdomain interface loop. These new structural features likely obstructed histo-blood group antigens, which are attachment factors for human norovirus, from binding at the equivalent sites on the feline GIV.2 P domain. Additionally, an ELISA showed that the feline GIV.2 was antigenically distinct from a human GII.10 norovirus. Structural analysis of a feline norovirus protruding domain.,Singh BK, Glatt S, Ferrer JL, Koromyslova AD, Leuthold MM, Dunder J, Hansman GS Virology. 2015 Jan 1;474:181-5. doi: 10.1016/j.virol.2014.10.028. Epub 2014 Nov, 19. PMID:25463616[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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