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Nat Struct Biol. 2000 Aug;7(8):693-9.

Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B.

Author information

1
Biology Department, Brookhaven National Laboratory, Upton, New York 11973, USA. swami@bnl.gov

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.

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PMID:
10932256
[Indexed for MEDLINE]

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