4Z92
crystal structure of parechovirus-1 virion
Summary for 4Z92
| Entry DOI | 10.2210/pdb4z92/pdb |
| Descriptor | capsid subunit VP1, Capsid subunit VP3, capsid subunit VP0, ... (4 entities in total) |
| Functional Keywords | parechovirus, picornavirus, virion, pathogen, virus |
| Biological source | Human parechovirus 1 (strain Harris) (HPeV-1) More |
| Total number of polymer chains | 4 |
| Total formula weight | 88219.17 |
| Authors | Kalynych, S.,Palkova, L.,Plevka, P. (deposition date: 2015-04-09, release date: 2015-11-18, Last modification date: 2024-01-10) |
| Primary citation | Kalynych, S.,Palkova, L.,Plevka, P. The Structure of Human Parechovirus 1 Reveals an Association of the RNA Genome with the Capsid. J.Virol., 90:1377-1386, 2015 Cited by PubMed Abstract: Parechoviruses are human pathogens that cause diseases ranging from gastrointestinal disorders to encephalitis. Unlike those of most picornaviruses, parechovirus capsids are composed of only three subunits: VP0, VP1, and VP3. Here, we present the structure of a human parechovirus 1 (HPeV-1) virion determined to a resolution of 3.1 Å. We found that interactions among pentamers in the HPeV-1 capsid are mediated by the N termini of VP0s, which correspond to the capsid protein VP4 and the N-terminal part of the capsid protein VP2 of other picornaviruses. In order to facilitate delivery of the virus genome into the cytoplasm, the N termini of VP0s have to be released from contacts between pentamers and exposed at the particle surface, resulting in capsid disruption. A hydrophobic pocket, which can be targeted by capsid-binding antiviral compounds in many other picornaviruses, is not present in HPeV-1. However, we found that interactions between the HPeV-1 single-stranded RNA genome and subunits VP1 and VP3 in the virion impose a partial icosahedral ordering on the genome. The residues involved in RNA binding are conserved among all parechoviruses, suggesting a putative role of the genome in virion stability or assembly. Therefore, putative small molecules that could disrupt HPeV RNA-capsid protein interactions could be developed into antiviral inhibitors. PubMed: 26581987DOI: 10.1128/JVI.02346-15 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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