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PDBsum entry 6t4c
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Contents |
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271 a.a.
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244 a.a.
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243 a.a.
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48 a.a.
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References listed in PDB file
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Key reference
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Title
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Glutathione facilitates enterovirus assembly by binding at a druggable pocket.
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Authors
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H.M.E.Duyvesteyn,
J.Ren,
T.S.Walter,
E.E.Fry,
D.I.Stuart.
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Ref.
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Commun Biol, 2020,
3,
9.
[DOI no: ]
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PubMed id
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Abstract
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Enteroviruses cause a range of human and animal diseases, some life-threatening,
but there remain no licenced anti-enterovirus drugs. However, a
benzene-sulfonamide derivative and related compounds have been shown recently to
block infection of a range of enteroviruses by binding the capsid at a
positively-charged surface depression conserved across many enteroviruses. It
has also been established that glutathione is essential for the assembly of many
enteroviruses, interacting with the capsid proteins to facilitate the formation
of the pentameric assembly intermediate, although the mechanism is unknown. Here
we show, by high resolution structure analyses of enterovirus F3, that reduced
glutathione binds to the same interprotomer pocket as the benzene-sulfonamide
derivative. Bound glutathione makes strong interactions with adjacent protomers,
thereby explaining the underlying biological role of this druggable binding
pocket and delineating the pharmacophore for potential antivirals.
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