期刊
NATURE COMMUNICATIONS
卷 4, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms3058
关键词
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资金
- Swedish Research Council [2010-5200]
- Wenner-Gren Foundations
- Swedish Foundation for Strategic research
- EMBO Long Term Fellowship
- Marie Curie Actions [EMBOCOFUND2010, GA-2010-267146]
- NIH [8P51OD011103-51, 1R56AI097834-01, 1R01NS080833-01]
- Swiss Light Source, Switzerland
Botulinum neurotoxins are highly toxic, and bind two receptors to achieve their high affinity and specificity for neurons. Here we present the first structure of a botulinum neurotoxin bound to both its receptors. We determine the 2.3-angstrom structure of a ternary complex of botulinum neurotoxin type B bound to both its protein receptor synaptotagmin II and its ganglioside receptor GD1a. We show that there is no direct contact between the two receptors, and that the binding affinity towards synaptotagmin II is not influenced by the presence of GD1a. The interactions of botulinum neurotoxin type B with the sialic acid 5 moiety of GD1a are important for the ganglioside selectivity. The structure demonstrates that the protein receptor and the ganglioside receptor occupy nearby but separate binding sites, thus providing two independent anchoring points.
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