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PDBsum entry 1d0h
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The structures of the h(c) fragment of tetanus toxin with carbohydrate subunit complexes provide insight into ganglioside binding.
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Authors
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P.Emsley,
C.Fotinou,
I.Black,
N.F.Fairweather,
I.G.Charles,
C.Watts,
E.Hewitt,
N.W.Isaacs.
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Ref.
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J Biol Chem, 2000,
275,
8889-8894.
[DOI no: ]
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PubMed id
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Abstract
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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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Figure 1.
Fig. 1. The overall fold of TeNT H[C]. The protein is
composed of two domains, a lentil lectin-like amino-terminal
domain and a  -trefoil
carboxyl-terminal domain.
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Figure 5.
Fig. 5. A stereo view, in the same orientation as Fig. 1,
of the positions of the carbohydrate units with respect to TeNT
H[C]. The carbohydrate units bind in four distinct sites, and
their positions and orientations make it unlikely that these
would correspond to a single ganglioside binding to a single
H[C] protein.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2000,
275,
8889-8894)
copyright 2000.
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Secondary reference #1
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Title
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Structure of the receptor binding fragment hc of tetanus neurotoxin.
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Authors
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T.C.Umland,
L.M.Wingert,
S.Swaminathan,
W.F.Furey,
J.J.Schmidt,
M.Sax.
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Ref.
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Nat Struct Biol, 1997,
4,
788-792.
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PubMed id
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