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

Paul Emsley; Constantina Fotinou; Isobel Black; Neil F. Fairweather; Ian G. Charles; Colin Watts; Eric Hewitt; Neil W. Isaacs

doi:10.1074/jbc.275.12.8889

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

Paul Emsley
, Constantina Fotinou
, Isobel Black
, Neil F. Fairweather
, Ian G. Charles
, Colin Watts
, Eric Hewitt
, Neil W. Isaacs (Lead / Corresponding author)

Research output: Contribution to journal › Article › peer-review

144 Citations (Scopus)

71 Downloads (Pure)

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.

Original language	English
Pages (from-to)	8889-8894
Number of pages	6
Journal	Journal of Biological Chemistry
Volume	275
Issue number	12
DOIs	https://doi.org/10.1074/jbc.275.12.8889
Publication status	Published - 24 Mar 2000

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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10.1074/jbc.275.12.8889Licence: CC BY

Final published versionFinal published version, 785 KBLicence: CC BY

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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.",

author = "Paul Emsley and Constantina Fotinou and Isobel Black and Fairweather, \{Neil F.\} and Charles, \{Ian G.\} and Colin Watts and Eric Hewitt and Isaacs, \{Neil W.\}",

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T1 - The structures of the H(C) fragment of tetanus toxin with carbohydrate subunit complexes provide insight into ganglioside binding

AU - Emsley, Paul

AU - Fotinou, Constantina

AU - Black, Isobel

AU - Fairweather, Neil F.

AU - Charles, Ian G.

AU - Watts, Colin

AU - Hewitt, Eric

AU - Isaacs, Neil W.

PY - 2000/3/24

Y1 - 2000/3/24

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0034708794

U2 - 10.1074/jbc.275.12.8889

DO - 10.1074/jbc.275.12.8889

M3 - Article

C2 - 10722735

AN - SCOPUS:0034708794

SN - 0021-9258

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EP - 8894

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 12

ER -

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

Abstract

ASJC Scopus subject areas

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