The structure of botulinum neurotoxin type B (BoNT/B) is analyzed, and it is demonstrated that the carbonyl oxygen of the scissile bond comes close to the zinc ion to form a Michaelis complex. The hydrated carbonyl is activated by the nucleophilic water, which moves closer to Glu 230 to form hydroge
NMR analysis of structure and function of snake neurotoxins
โ Scribed by Tatsuo Miyazawa; Toshiya Endo; Fuyuhiko Inagaki; Kyozo Hayashi; Nobuo Tamiya
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1983
- Tongue
- English
- Weight
- 374 KB
- Volume
- 22
- Category
- Article
- ISSN
- 0006-3525
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โฆ Synopsis
The 270-MHz proton-nmr spectra of short neurotoxins (erabutoxins from Laticauda semifasciata and cobrotoxin from Naja naja atra) and long neurotoxins (toxin B from Naja naja and a-bungarotoxin from Bungarus multicinctus) have been analyzed. The conformation of erabutoxin b in solution is largely consistent with the x-ray crystal analysis, although the environment of His-7 in solution is definitely different from that in the crystal. The pH-dependent transition has been found for toxin B, indicating that the conformation in neutral solution is different from that in the crystal as grown from acidic solution. The deuterium-exchange rates of the amide protons for the four neurotoxins have been measured. The order of structural rigidity is the same as the order of the irreversibility of neuromuscular block by neurotoxins.
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