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Toxicon. 2009 Oct;54(5):550-60. doi: 10.1016/j.toxicon.2008.12.027. Epub 2009 Mar 4.

Receptor and substrate interactions of clostridial neurotoxins.

Author information

1
The Howard Hughes Medical Institute and Departments of Molecular and Cellular Physiology, Neurology and Neurological Sciences, Structural Biology, and Photon Science, Stanford University, J.H. Clark Center, E300C, 318 Campus Drive, Stanford, CA 94305, USA. brunger@stanford.edu

Abstract

The high potency of clostridial neurotoxins relies predominantly on their neurospecific binding and specific hydrolysis of SNARE proteins. Their multi-step mode of mechanism can be ascribed to their multi-domain three-dimensional structure. The C-terminal H(CC)-domain interacts subsequently with complex polysialo-gangliosides such as GT1b and a synaptic vesicle protein receptor via two neighbouring binding sites, resulting in highly specific uptake of the neurotoxins at synapses of cholinergic motoneurons. After its translocation the enzymatically active light chain specifically hydrolyses specific SNARE proteins, preventing SNARE complex assembly and thereby blocking exocytosis of neurotransmitter.

PMID:
19268493
PMCID:
PMC2756235
DOI:
10.1016/j.toxicon.2008.12.027
[Indexed for MEDLINE]
Free PMC Article
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