Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity
Rongsheng Jin,
Andreas Rummel,
Thomas Binz and
Axel T. Brunger ()
Additional contact information
Rongsheng Jin: Howard Hughes Medical Institute
Andreas Rummel: Institut für Toxikologie
Thomas Binz: Institut für Biochemie, Medizinische Hochschule Hannover
Axel T. Brunger: Howard Hughes Medical Institute
Nature, 2006, vol. 444, issue 7122, 1092-1095
Abstract:
Botulism toxin Botulinum toxins, produced by Clostridia botulinum, are a potential biological hazard to humans and a potential bioweapons threat. The toxins are potent inhibitors of neurotransmitter release at synapses, and it is this property that causes the neuroparalytic syndrome known as botulism. Two related papers now report the crystal structure of botulinum toxin B bound to its receptor on the exposed surface of the neuron. This will provide insight into the high affinity and specificity of this interaction, and aid in the development of antibotulism vaccines and drugs.
Date: 2006
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DOI: 10.1038/nature05387
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