Abstract
Clostridium botulinum neurotoxins are among the most potent toxins to humans. The crystal structures of intact C. botulinum neurotoxin type B (BoNT/B) and its complex with sialyllactose, determined at 1. 8 and 2.6 A resolution, respectively, provide insight into its catalytic and binding sites. The position of the belt region in BoNT/B is different from that in BoNT/A; this observation presents interesting possibilities for designing specific inhibitors that could be used to block the activity of this neurotoxin. The structures of BoNT/B and its complex with sialyllactose provide a detailed description of the active site and a model for interactions between the toxin and its cell surface receptor. The latter may provide valuable information for recombinant vaccine development.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Binding Sites
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Botulinum Toxins / chemistry*
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Botulinum Toxins / metabolism*
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Botulinum Toxins, Type A / chemistry
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Botulinum Toxins, Type A / metabolism
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Catalytic Domain*
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Clostridium botulinum / chemistry*
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Crystallography, X-Ray
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Gangliosides / metabolism
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Lactose / analogs & derivatives
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Lactose / chemistry
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Lactose / metabolism
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Models, Molecular
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Molecular Sequence Data
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Receptors, Cell Surface / chemistry
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Receptors, Cell Surface / metabolism
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Sequence Alignment
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Sialic Acids / chemistry
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Sialic Acids / metabolism
Substances
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Gangliosides
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Receptors, Cell Surface
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Sialic Acids
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rimabotulinumtoxinB
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N-acetylneuraminoyllactose
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Botulinum Toxins
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Botulinum Toxins, Type A
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Lactose