1DFQ
THE HC FRAGMENT OF TETANUS TOXIN COMPLEXED WITH SIALIC ACID
Summary for 1DFQ
Entry DOI | 10.2210/pdb1dfq/pdb |
Related | 1A8D 1AF9 1D0H 1DIW |
Descriptor | TETANUS TOXIN HC, N-acetyl-beta-neuraminic acid (3 entities in total) |
Functional Keywords | beta trefoil, jelly-roll, toxin, carbohydrate |
Biological source | Clostridium tetani |
Total number of polymer chains | 1 |
Total formula weight | 51144.49 |
Authors | Emsley, P.,Fotinou, C.,Black, I.,Fairweather, N.F.,Charles, I.G.,Watts, C.,Hewitt, E.,Isaacs, N.W. (deposition date: 1999-11-20, release date: 2000-03-24, Last modification date: 2024-02-07) |
Primary citation | Emsley, P.,Fotinou, C.,Black, I.,Fairweather, N.F.,Charles, I.G.,Watts, C.,Hewitt, E.,Isaacs, N.W. The structures of the H(C) fragment of tetanus toxin with carbohydrate subunit complexes provide insight into ganglioside binding. J.Biol.Chem., 275:8889-8894, 2000 Cited by PubMed 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. PubMed: 10722735DOI: 10.1074/jbc.275.12.8889 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
Download full validation report