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Structure-Function Relationship of Botulinum and Tetanus Neurotoxins

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Botulinum and Tetanus Neurotoxins

Abstract

Botulinum and tetanus neurotoxins belong to a general group of bacterial protein toxins with a distinctive characteristics in terms of three structural domains with different complementary functions (Fig. 1). Other toxins of this group include cholera, diphtheria and Pseudomonas exotoxin A. These toxins have a polypeptide segment devoted to establish the binding with the target cell, apolypeptide segment that primarily helps translocate the whole or apart of the toxin across the cell membrane, and a third polypeptide segment which possesses an enzymatic or other putative biological activity capable of interfering with certain biochemical reactions within its target cells. Although the third domain elicits the ultimate toxic action, the other two domains are equally important for the biological action of the cellular toxicity of this group of toxins.

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Authors and Affiliations

  1. Department of Chemistry, University of Massachusetts at Dartmouth, N. Dartmouth, MA, 02747, USA

    Bal Ram Singh

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  1. Bal Ram Singh
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Editor information

Editors and Affiliations

  1. University of Wisconsin, Madison, Wisconsin, USA

    Bibhuti R. DasGupta

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© 1993 Springer Science+Business Media New York

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Singh, B.R. (1993). Structure-Function Relationship of Botulinum and Tetanus Neurotoxins. In: DasGupta, B.R. (eds) Botulinum and Tetanus Neurotoxins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9542-4_41

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  • DOI: https://doi.org/10.1007/978-1-4757-9542-4_41

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4757-9544-8

  • Online ISBN: 978-1-4757-9542-4

  • eBook Packages: Springer Book Archive

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