View source for 6ohw


==Structural basis for human coronavirus attachment to sialic acid receptors. Apo-HCoV-OC43 S==
<SX load='6ohw' size='340' side='right' viewer='molstar' caption='[[6ohw]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ohw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_coronavirus_OC43 Human coronavirus OC43]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OHW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OHW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=6ohw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ohw OCA], [https://pdbe.org/6ohw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ohw RCSB], [https://www.ebi.ac.uk/pdbsum/6ohw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ohw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q696P8_CVHOC Q696P8_CVHOC] 
<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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ohw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</SX>
[[Category: Human coronavirus OC43]]
[[Category: Large Structures]]
[[Category: Boons GJ]]
[[Category: Bosch BJ]]
[[Category: Koerhuis D]]
[[Category: Lang Y]]
[[Category: Li Z]]
[[Category: Rey FA]]
[[Category: Tortorici MA]]
[[Category: Veesler D]]
[[Category: Walls AC]]
[[Category: Wang C]]
[[Category: De Groot R]]