PROSITE documentation PDOC00245Snake toxins signature
Snake toxins belong to a family of proteins [1,2,3] which groups short and long neurotoxins, cytotoxins and short toxins, as well as a other miscellanous venom peptides. Most of these toxins act by binding to the nicotinic acetylcholine receptors in the postsynaptic membrane of skeletal muscles and prevent the binding of acetylcholine, thereby blocking the excitation of muscles.
Snake toxins are proteins that consist of sixty to seventy five amino acids. Among the invariant residues are eight cysteines all involved in disulfide bonds. A signature pattern was developed [4] which includes four of these cysteines as well as a conserved proline thought to be important for the maintenance of the tertiary structure. The second cysteine in the pattern is linked to the third one by a disulfide bond.
Last update:May 2004 / Text revised.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Dufton M.J. |
| Title | Classification of elapid snake neurotoxins and cytotoxins according to chain length: evolutionary implications. | |
| Source | J. Mol. Evol. 20:128-134(1984). | |
| PubMed ID | 6433031 |
| 2 | Authors | Endo T. Tamiya N. |
| Source | (In) Snake toxins, Harvey A.L., Ed., pp165-222, Pergamon Press, New-York, (1991). |
| 3 | Authors | Mebs D. Claus I. |
| Source | (In) Snake toxins, Harvey A.L., Ed., pp425-447, Pergamon Press, New-York, (1991). |
| 4 | Authors | Jonassen I. Collins J.F. Higgins D.G. |
| Source | Protein Sci. 4:1587-1595(1995). |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)