5JZG
CryoEM structure of the native empty particle of a human rhinovirus C
Summary for 5JZG
Entry DOI | 10.2210/pdb5jzg/pdb |
Related | 5K0U |
EMDB information | 8184 8189 |
Descriptor | Capsid protein VP1, Capsid protein VP3, Capsid protein VP0 (3 entities in total) |
Functional Keywords | virus, jelly roll |
Biological source | Rhinovirus C More |
Total number of polymer chains | 3 |
Total formula weight | 94015.00 |
Authors | Liu, Y.,Hill, M.G.,Klose, T.,Chen, Z.,Watters, K.E.,Jiang, W.,Palmenberg, A.C.,Rossmann, M.G. (deposition date: 2016-05-16, release date: 2016-07-13, Last modification date: 2024-03-06) |
Primary citation | Liu, Y.,Hill, M.G.,Klose, T.,Chen, Z.,Watters, K.,Bochkov, Y.A.,Jiang, W.,Palmenberg, A.C.,Rossmann, M.G. Atomic structure of a rhinovirus C, a virus species linked to severe childhood asthma. Proc.Natl.Acad.Sci.USA, 113:8997-9002, 2016 Cited by PubMed Abstract: Isolates of rhinovirus C (RV-C), a recently identified Enterovirus (EV) species, are the causative agents of severe respiratory infections among children and are linked to childhood asthma exacerbations. The RV-C have been refractory to structure determination because they are difficult to propagate in vitro. Here, we report the cryo-EM atomic structures of the full virion and native empty particle (NEP) of RV-C15a. The virus has 60 "fingers" on the virus outer surface that probably function as dominant immunogens. Because the NEPs also display these fingers, they may have utility as vaccine candidates. A sequence-conserved surface depression adjacent to each finger forms a likely binding site for the sialic acid on its receptor. The RV-C, unlike other EVs, are resistant to capsid-binding antiviral compounds because the hydrophobic pocket in VP1 is filled with multiple bulky residues. These results define potential molecular determinants for designing antiviral therapeutics and vaccines. PubMed: 27511920DOI: 10.1073/pnas.1606595113 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.16 Å) |
Structure validation
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