3NXD
JC polyomavirus VP1 in complex with LSTc
Summary for 3NXD
| Entry DOI | 10.2210/pdb3nxd/pdb |
| Related | 1vps 3NXG 3bwr |
| Descriptor | Major capsid protein VP1, N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | beta-sandwich with jelly roll topology, major capsid protein, viral protein |
| Biological source | JC polyomavirus (JCPyV) |
| Cellular location | Virion: P03089 |
| Total number of polymer chains | 5 |
| Total formula weight | 153209.95 |
| Authors | Neu, U.,Stroeh, L.J.,Stehle, T. (deposition date: 2010-07-13, release date: 2010-11-17, Last modification date: 2024-02-21) |
| Primary citation | Neu, U.,Maginnis, M.S.,Palma, A.S.,Stroh, L.J.,Nelson, C.D.,Feizi, T.,Atwood, W.J.,Stehle, T. Structure-function analysis of the human JC polyomavirus establishes the LSTc pentasaccharide as a functional receptor motif. Cell Host Microbe, 8:309-319, 2010 Cited by PubMed Abstract: The human JC polyomavirus (JCV) causes a fatal demyelinating disease, progressive multifocal leukoencephalopathy (PML), in immunocompromised individuals. Current treatment options for PML are inadequate. Sialylated oligosaccharides and the serotonin receptor are known to be necessary for JCV entry, but the molecular interactions underlying JCV attachment remain unknown. Using glycan array screening and viral infectivity assays, we identify a linear sialylated pentasaccharide with the sequence NeuNAc-α2,6-Gal-β1,4-GlcNAc-β1,3-Gal-β1,4-Glc (LSTc) present on host glycoproteins and glycolipids as a specific JCV recognition motif. The crystal structure of the JCV capsid protein VP1 was solved alone and in complex with LSTc. It reveals extensive interactions with the terminal sialic acid of the LSTc motif and specific recognition of an extended conformation of LSTc. Mutations in the JCV oligosaccharide-binding sites abolish cell attachment, viral spread, and infectivity, further validating the importance of this interaction. Our findings provide a powerful platform for the development of antiviral compounds. PubMed: 20951965DOI: 10.1016/j.chom.2010.09.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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