6NZK
Structural basis for human coronavirus attachment to sialic acid receptors
Summary for 6NZK
| Entry DOI | 10.2210/pdb6nzk/pdb |
| EMDB information | 0557 |
| Descriptor | Spike surface glycoprotein, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | coronavirus spike glycoprotein, sialic acid, hcov-oc43, fusion protein, viral protein |
| Biological source | Human coronavirus OC43 (HCoV-OC43) |
| Total number of polymer chains | 3 |
| Total formula weight | 460838.89 |
| Authors | Tortorici, M.A.,Walls, A.C.,Lang, Y.,Wang, C.,Li, Z.,Koerhuis, D.,Boons, G.J.,Bosch, B.J.,Rey, F.A.,de Groot, R.,Veesler, D. (deposition date: 2019-02-13, release date: 2019-06-05, Last modification date: 2024-11-06) |
| Primary citation | Alejandra Tortorici, M.,Walls, A.C.,Lang, Y.,Wang, C.,Li, Z.,Koerhuis, D.,Boons, G.J.,Bosch, B.J.,Rey, F.A.,de Groot, R.J.,Veesler, D. Structural basis for human coronavirus attachment to sialic acid receptors. Nat.Struct.Mol.Biol., 26:481-489, 2019 Cited by PubMed Abstract: 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. PubMed: 31160783DOI: 10.1038/s41594-019-0233-y PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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