Abstract
Enterovirus 71 is a picornavirus associated with fatal neurological illness in infants and young children. Here, we report the crystal structure of enterovirus 71 and show that, unlike in other enteroviruses, the "pocket factor," a small molecule that stabilizes the virus, is partly exposed on the floor of the "canyon." Thus, the structure of antiviral compounds may require a hydrophilic head group designed to interact with residues at the entrance of the pocket.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Capsid / chemistry
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Capsid / metabolism
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Capsid / ultrastructure
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Capsid Proteins / chemistry*
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Capsid Proteins / metabolism
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Crystallography, X-Ray
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Enterovirus A, Human / chemistry*
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Enterovirus A, Human / metabolism
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Enterovirus A, Human / ultrastructure*
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Humans
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Hydrophobic and Hydrophilic Interactions
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Models, Molecular
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Protein Conformation
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Receptors, Virus / metabolism
Substances
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Capsid Proteins
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Receptors, Virus