6nzk
From Proteopedia
(Difference between revisions)
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==Structural basis for human coronavirus attachment to sialic acid receptors== | ==Structural basis for human coronavirus attachment to sialic acid receptors== | ||
| - | <StructureSection load='6nzk' size='340' side='right'caption='[[6nzk]], [[Resolution|resolution]] 2. | + | <StructureSection load='6nzk' size='340' side='right'caption='[[6nzk]], [[Resolution|resolution]] 2.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6nzk]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NZK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NZK FirstGlance]. <br> | <table><tr><td colspan='2'>[[6nzk]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NZK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NZK FirstGlance]. <br> | ||
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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=6nzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nzk OCA], [http://pdbe.org/6nzk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nzk RCSB], [http://www.ebi.ac.uk/pdbsum/6nzk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nzk 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=6nzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nzk OCA], [http://pdbe.org/6nzk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nzk RCSB], [http://www.ebi.ac.uk/pdbsum/6nzk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nzk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Coronaviruses cause respiratory tract infections in humans and outbreaks of deadly pneumonia worldwide. Infections are initiated by the transmembrane spike (S) glycoprotein, which binds to host receptors and fuses the viral and cellular membranes. To understand the molecular basis of coronavirus attachment to oligosaccharide receptors, we determined cryo-EM structures of coronavirus OC43 S glycoprotein trimer in isolation and in complex with a 9-O-acetylated sialic acid. We show that the ligand binds with fast kinetics to a surface-exposed groove and that interactions at the identified site are essential for S-mediated viral entry into host cells, but free monosaccharide does not trigger fusogenic conformational changes. The receptor-interacting site is conserved in all coronavirus S glycoproteins that engage 9-O-acetyl-sialogycans, with an architecture similar to those of the ligand-binding pockets of coronavirus hemagglutinin esterases and influenza virus C/D hemagglutinin-esterase fusion glycoproteins. Our results demonstrate these viruses evolved similar strategies to engage sialoglycans at the surface of target cells. | ||
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| + | Structural basis for human coronavirus attachment to sialic acid receptors.,Alejandra Tortorici M, Walls AC, Lang Y, Wang C, Li Z, Koerhuis D, Boons GJ, Bosch BJ, Rey FA, de Groot RJ, Veesler D Nat Struct Mol Biol. 2019 Jun;26(6):481-489. doi: 10.1038/s41594-019-0233-y. Epub, 2019 Jun 3. PMID:31160783<ref>PMID:31160783</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6nzk" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:35, 19 June 2019
Structural basis for human coronavirus attachment to sialic acid receptors
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