| Literature References | 1. KOPEYAN, C., MANSUELLE, P., SAMPIERI, F., BRANDO, T., BAHRAOUI, E.M.,
ROCHAT, H. AND GRANIER, C.
Primary structure of scorpion anti-insect toxins isolated from the venom
of Leiurus quiquestriatus quinquestriatus.
FEBS LETT. 261 423-426 (1990).
2. GREGOIRE, J. AND ROCHAT, H.
Covalent structure of toxins I and II from the scorpion Buthus occitanus
tunetanus.
TOXICON. 21 153-162 (1983).
3. ZHOU, X.H., YANG, D., ZHANG, J.H., LIU, C.M. AND LEI, K.J.
Purification and N-terminal partial sequence of anti-epilepsy peptide
from venom of the scorpion Buthus martensii Karsch.
BIOCHEM.J. 257 509-517 (1989).
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| Documentation | Scorpion toxins, which may be mammal or insect specific, bind to sodium
channels, inhibiting the inactivation of activated channels and blocking
neuronal transmission. The complete covalent structure of the toxins has
been deduced: it comprises around 66 amino acid residues and is cross-
linked by 4 disulphide bridges [1,2]. An anti-epilepsy peptide isolated
from scorpion venom [3] shows similarity to both scorpion neurotoxins
and anti-insect toxins.
SCORPNTOXIN is a 4-element fingerprint that provides a signature for the
scorpion toxins. The fingerprint was derived from an initial alignment
of 11 sequences: the motifs were drawn from virtually the full alignment
length, and encode 7 well-conserved Cys residues. Three iterations on
OWL23.2 were required to reach convergence, at which point a true set
comprising 37 sequences was identified. Several partial matches were also
found, many of which are fragments.
An update on SPTR37_9f identified a true set of 49 sequences, and 20
partial matches.
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