The structures of the H(C) fragment of tetanus toxin with carbohydrate subunit complexes provide insight into ganglioside binding.
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.
Emsley
P
P
Department of Chemistry, University of Glasgow, Glasgow G12 8QQ, United Kingdom.
Fotinou
C
C
Black
I
I
Fairweather
N F
NF
Charles
I G
IG
Watts
C
C
Hewitt
E
E
Isaacs
N W
NW
D000116:Acetylgalactosamine / Q000737:chemistry; D001665:Binding Sites; D002241:Carbohydrates / Q000737:chemistry*; D018360:Crystallography, X-Ray; D005690:Galactose / Q000737:chemistry; D005732:Gangliosides / Q000378:metabolism*; D007785:Lactose / Q000737:chemistry; D008958:Models, Molecular; D019158:N-Acetylneuraminic Acid / Q000737:chemistry; D010446:Peptide Fragments / Q000737:chemistry*; D011485:Protein Binding; D013744:Tetanus Toxin / Q000737:chemistry* / Q000378:metabolism
D002241:Carbohydrates; D005732:Gangliosides; D010446:Peptide Fragments; D013744:Tetanus Toxin; D019158:N-Acetylneuraminic Acid; D007785:Lactose; D000116:Acetylgalactosamine; D005690:Galactose