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3VBS

Crystal structure of human Enterovirus 71

Summary for 3VBS
Entry DOI10.2210/pdb3vbs/pdb
Related3VBF 3VBH 3VBO 3VBR 3VBU
DescriptorGenome Polyprotein, capsid protein VP1, Genome Polyprotein, capsid protein VP2, Genome Polyprotein, capsid protein VP3, ... (5 entities in total)
Functional Keywordsvirus, hand-foot-and-mouth disease, enterovirus uncoating, pocket factor, adaptor-sensor, icosahedral virus
Biological sourceHuman enterovirus 71
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Total number of polymer chains4
Total formula weight92750.80
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 citationWang, 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: 22388738
DOI: 10.1038/nsmb.2255
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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