The structures of the H(C) fragment of tetanus toxin with carbohydrate subunit complexes provide insight into ganglioside binding

Paul Emsley, Constantina Fotinou, Isobel Black, Neil F. Fairweather, Ian G. Charles, Colin Watts, Eric Hewitt, Neil W. Isaacs (Lead / Corresponding author)

    Research output: Contribution to journalArticlepeer-review

    140 Citations (Scopus)
    33 Downloads (Pure)

    Abstract

    The entry of tetanus neurotoxin into neuronal cells proceeds through the initial binding of the toxin to gangliosides on the cell surface. The carboxyl-terminal fragment of the heavy chain of tetanus neurotoxin contains the ganglioside-binding site, which has not yet been fully characterized. The crystal structures of native H(c) and of H(c) soaked with carbohydrates reveal a number of binding sites and provide insight into the possible mode of ganglioside binding.

    Original languageEnglish
    Pages (from-to)8889-8894
    Number of pages6
    JournalJournal of Biological Chemistry
    Volume275
    Issue number12
    DOIs
    Publication statusPublished - 24 Mar 2000

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology

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