The structures of the H(C) fragment of tetanus toxin with carbohydrate subunit complexes provide insight into ganglioside binding.

Emsley, P; Fotinou, C; Black, I; Fairweather, NF; Charles, IG; Watts, C; Hewitt, E; Isaacs, NW

The structures of the H(C) fragment of tetanus toxin with carbohydrate subunit complexes provide insight into ganglioside binding.

Emsley, P Fotinou, C Black, I Fairweather, NF Charles, IG Watts, C Hewitt, E Isaacs, NW

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Publication Type:: Journal Article
Citation:: J Biol Chem, 2000, 275 (12), pp. 8889 - 8894
Issue Date:: 2000-03-24

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Field	Value	Language
dc.contributor.author	Emsley, P	en_US
dc.contributor.author	Fotinou, C	en_US
dc.contributor.author	Black, I	en_US
dc.contributor.author	Fairweather, NF	en_US
dc.contributor.author	Charles, IG	en_US
dc.contributor.author	Watts, C	en_US
dc.contributor.author	Hewitt, E	en_US
dc.contributor.author	Isaacs, NW	en_US
dc.date.issued	2000-03-24	en_US
dc.identifier.citation	J Biol Chem, 2000, 275 (12), pp. 8889 - 8894	en_US
dc.identifier.issn	0021-9258	en_US
dc.identifier.uri	http://hdl.handle.net/10453/13275
dc.description.abstract	The entry of tetanus neurotoxin into neuronal cells proceeds through the initial binding of the toxin to gangliosides on the cell surface. The carboxyl-terminal fragment of the heavy chain of tetanus neurotoxin contains the ganglioside-binding site, which has not yet been fully characterized. The crystal structures of native H(C) and of H(C) soaked with carbohydrates reveal a number of binding sites and provide insight into the possible mode of ganglioside binding.	en_US
dc.language	eng	en_US
dc.relation.ispartof	J Biol Chem	en_US
dc.relation.isbasedon	10.1074/jbc.275.12.8889	en_US
dc.subject.classification	Biochemistry & Molecular Biology	en_US
dc.subject.mesh	N-Acetylneuraminic Acid	en_US
dc.subject.mesh	Carbohydrates	en_US
dc.subject.mesh	Acetylgalactosamine	en_US
dc.subject.mesh	Gangliosides	en_US
dc.subject.mesh	Galactose	en_US
dc.subject.mesh	Lactose	en_US
dc.subject.mesh	Peptide Fragments	en_US
dc.subject.mesh	Tetanus Toxin	en_US
dc.subject.mesh	Crystallography, X-Ray	en_US
dc.subject.mesh	Binding Sites	en_US
dc.subject.mesh	Protein Binding	en_US
dc.subject.mesh	Models, Molecular	en_US
dc.title	The structures of the H(C) fragment of tetanus toxin with carbohydrate subunit complexes provide insight into ganglioside binding.	en_US
dc.type	Journal Article
utslib.citation.volume	12	en_US
utslib.citation.volume	275	en_US
utslib.location.activity	United States	en_US
utslib.for	0601 Biochemistry and Cell Biology	en_US
utslib.for	03 Chemical Sciences	en_US
utslib.for	06 Biological Sciences	en_US
utslib.for	11 Medical and Health Sciences	en_US
dc.location.activity	ISI:000086507700085	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - ithree - Institute of Infection, Immunity and Innovation
utslib.copyright.status	closed_access
pubs.issue	12	en_US
pubs.publication-status	Published	en_US
pubs.volume	275	en_US

Abstract:

The entry of tetanus neurotoxin into neuronal cells proceeds through the initial binding of the toxin to gangliosides on the cell surface. The carboxyl-terminal fragment of the heavy chain of tetanus neurotoxin contains the ganglioside-binding site, which has not yet been fully characterized. The crystal structures of native H(C) and of H(C) soaked with carbohydrates reveal a number of binding sites and provide insight into the possible mode of ganglioside binding.

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http://hdl.handle.net/10453/13275