1EPW

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

(2000) Nat Struct Biol 7: 693-699

• PubMed: 10932256 Search on PubMed
• DOI: https://doi.org/10.1038/78005
• Primary Citation of Related Structures:  
  1EPW, 1F31


• PubMed 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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Organizational Affiliation: 

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