8.B.20 The Australian Scorpion Toxin (Liotoxin) Family

The three-disulfide inhibitor cystine knot (ICK) motif is a fold common to venom peptides from spiders, scorpions, and aquatic cone snails. It has been proposed that the ICK motif is an elaboration of an ancestral two-disulfide fold coined the disulfide-directed β-hairpin (DDH). Smith et al. 2011 reported the isolation, characterization, and structure of a novel toxin [U(1)-liotoxin-Lw1a (U(1)-LITX-Lw1a)] (Liotoxin) from the venom of the scorpion Liocheles waigiensis. It is the first example of a native peptide that adopts the DDH fold. Liotoxin not only represents the discovery of a missing link in venom protein evolution, it is the first member of a fourth structural fold to be adopted by scorpion-venom peptides. Additionally, Smith et al. 2011 showed that Liotoxin has potent insecticidal activity across a broad range of insect pest species, thereby providing a unique structural scaffold for bioinsecticide development.  It appears to impair the activities of ryanodine-sensitive Ca2+ release channels.


This family belongs to the Conotoxin Superfamily.
 

References:

Smith, J.J., J.M. Hill, M.J. Little, G.M. Nicholson, G.F. King, and P.F. Alewood. (2011). Unique scorpion toxin with a putative ancestral fold provides insight into evolution of the inhibitor cystine knot motif. Proc. Natl. Acad. Sci. USA 108: 10478-10483.
Examples:

TC#NameOrganismal TypeExample
8.B.20.1.1

Liotoxin of 75 aas and 1 N-termina TMS.  The 3-d structure of a 36 aa peptide derived from Liotoxin has has been determined (2KYJ_A) (Smith et al. 2011).

Animals (scorpions)

Liotoxin of Liocheles waigiensis (Australian scorpion)

 
8.B.20.1.2

The Insecticidal toxin, OcyC10, of 75 aas.

Animals (scorpions)

OcyC10 of Opisthacanthus cayaporum