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PROSITE documentation PDOC00875 [for PROSITE entry PS01138] |
Scorpion venoms contain a variety of peptides toxic to mammals, insects and crustaceans. Among these peptides there is a family of short toxins (30 to 40 residues) [1,2] that currently consist of:
As shown in the following schematic representation, these toxins contain six conserved cysteines involved in disulfide bonds. Our signature pattern contains the last five cysteines.
+---------------------+ | | | ************************ xxxxxxxCxxxxxCxxxCxxxxxxxxxxxCxxxxCxCxxx | | | | | +----------------|-+ +--------------------+
'C': conserved cysteine involved in a disulfide bond. '*': position of the pattern.Note:
K+ channel inhibitors have a lysine before the second cysteine in the patterns, while the other toxins have a glutamine.
Last update:May 2004 / Text revised.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Martin B.M. Ramirez A.N. Gurrola G.B. Nobile M. Prestipino G. Possani L.D. |
Title | Novel K(+)-channel-blocking toxins from the venom of the scorpion Centruroides limpidus limpidus Karsch. | |
Source | Biochem. J. 304:51-56(1994). | |
PubMed ID | 7998956 |
2 | Authors | Lippens G. Najib J. Wodak S.J. Tartar A. |
Title | NMR sequential assignments and solution structure of chlorotoxin, a small scorpion toxin that blocks chloride channels. | |
Source | Biochemistry 34:13-21(1995). | |
PubMed ID | 7819188 |