3VBU
Crystal structure of empty human Enterovirus 71 particle
Summary for 3VBU
Entry DOI | 10.2210/pdb3vbu/pdb |
Related | 3VBF 3VBH 3VBO 3VBR 3VBS |
Descriptor | Genome Polyprotein, capsid protein VP1, Genome Polyprotein, capsid protein VP0, Genome Polyprotein, capsid protein VP3 (3 entities in total) |
Functional Keywords | virus, hand-foot-and-mouth disease, enterovirus uncoating, pocket factor, adaptor-sensor, icosahedral virus |
Biological source | Human enterovirus 71 More |
Total number of polymer chains | 3 |
Total formula weight | 77460.98 |
Authors | Wang, X.,Peng, W.,Ren, J.,Hu, Z.,Xu, J.,Lou, Z.,Li, X.,Yin, W.,Shen, X.,Porta, C.,Walter, T.S.,Evans, G.,Axford, D.,Owen, R.,Rowlands, D.J.,Wang, J.,Stuart, D.I.,Fry, E.E.,Rao, Z. (deposition date: 2012-01-02, release date: 2012-02-29, Last modification date: 2023-09-13) |
Primary citation | Wang, X.,Peng, W.,Ren, J.,Hu, Z.,Xu, J.,Lou, Z.,Li, X.,Yin, W.,Shen, X.,Porta, C.,Walter, T.S.,Evans, G.,Axford, D.,Owen, R.,Rowlands, D.J.,Wang, J.,Stuart, D.I.,Fry, E.E.,Rao, Z. A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71. Nat.Struct.Mol.Biol., 19:424-429, 2012 Cited by PubMed Abstract: Enterovirus 71 (EV71) is a major agent of hand, foot and mouth disease in children that can cause severe central nervous system disease and death. No vaccine or antiviral therapy is available. High-resolution structural analysis of the mature virus and natural empty particles shows that the mature virus is structurally similar to other enteroviruses. In contrast, the empty particles are markedly expanded and resemble elusive enterovirus-uncoating intermediates not previously characterized in atomic detail. Hydrophobic pockets in the EV71 capsid are collapsed in this expanded particle, providing a detailed explanation of the mechanism for receptor-binding triggered virus uncoating. These structures provide a model for enterovirus uncoating in which the VP1 GH loop acts as an adaptor-sensor for cellular receptor attachment, converting heterologous inputs to a generic uncoating mechanism, highlighting new opportunities for therapeutic intervention. PubMed: 22388738DOI: 10.1038/nsmb.2255 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (4 Å) |
Structure validation
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