5BNO
Crystal structure of human enterovirus D68 in complex with 6'SLN
Summary for 5BNO
| Entry DOI | 10.2210/pdb5bno/pdb |
| Related | 5BNN 5BNP |
| Related PRD ID | PRD_900046 |
| Descriptor | Capsid protein VP1, Capsid protein VP2, Capsid protein VP3, ... (6 entities in total) |
| Functional Keywords | enterovirus, capsid, beta jelly roll, virus, receptor |
| Biological source | Enterovirus D68 More |
| Total number of polymer chains | 4 |
| Total formula weight | 95704.95 |
| Authors | Liu, Y.,Sheng, J.,Meng, G.,Xiao, C.,Rossmann, M.G. (deposition date: 2015-05-26, release date: 2015-11-18, Last modification date: 2023-09-27) |
| Primary citation | Liu, Y.,Sheng, J.,Baggen, J.,Meng, G.,Xiao, C.,Thibaut, H.J.,van Kuppeveld, F.J.,Rossmann, M.G. Sialic acid-dependent cell entry of human enterovirus D68. Nat Commun, 6:8865-8865, 2015 Cited by PubMed Abstract: Human enterovirus D68 (EV-D68) is a causative agent of childhood respiratory diseases and has now emerged as a global public health threat. Nevertheless, knowledge of the tissue tropism and pathogenesis of EV-D68 has been hindered by a lack of studies on the receptor-mediated EV-D68 entry into host cells. Here we demonstrate that cell surface sialic acid is essential for EV-D68 to bind to and infect susceptible cells. Crystal structures of EV-D68 in complex with sialylated glycan receptor analogues show that they bind into the 'canyon' on the virus surface. The sialic acid receptor induces a cascade of conformational changes in the virus to eject a fatty-acid-like molecule that regulates the stability of the virus. Thus, virus binding to a sialic acid receptor and to immunoglobulin-like receptors used by most other enteroviruses share a conserved mechanism for priming viral uncoating and facilitating cell entry. PubMed: 26563423DOI: 10.1038/ncomms9865 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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