PROSITE documentation PDOC00875

Scorpion short toxins signature





Description

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:

  • Inhibitors of calcium-activated and/or voltage-dependent potassium channels such as charybdotoxin (ChTX), iberiotoxin (IbTX), kaliotoxin (KTX), leiurotoxin I (LeTX I), margatoxin (MgTX) or noxiustoxin (NTX)
  • Inhibitors of chloride channels such as chlorotoxin.
  • Insect toxins such as insectotoxin I1, insectotoxin I5a and neurotoxin P2.

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.

Technical section

PROSITE method (with tools and information) covered by this documentation:

SCORP_SHORT_TOXIN, PS01138; Scorpion short toxins signature  (PATTERN)


References

1AuthorsMartin B.M., Ramirez A.N., Gurrola G.B., Nobile M., Prestipino G., Possani L.D.
TitleNovel K(+)-channel-blocking toxins from the venom of the scorpion Centruroides limpidus limpidus Karsch.
SourceBiochem. J. 304:51-56(1994).
PubMed ID7998956

2AuthorsLippens G., Najib J., Wodak S.J., Tartar A.
TitleNMR sequential assignments and solution structure of chlorotoxin, a small scorpion toxin that blocks chloride channels.
SourceBiochemistry 34:13-21(1995).
PubMed ID7819188



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