HgeTx1
HgeTx1 (systematic name:
Etymology and Source
[edit]The toxin HgeTx1 is produced by the Mexican scorpion Hoffmanihadrurus gertschi, which belongs to the family of Caraboctonidae.[1]
HgeTx1 is the first toxin (Tx1) from this scorpion (Hge).[2] HgeTx1 belongs to the
Chemical Structure
[edit]All
Target
[edit]Electrophysiological experiments (whole cell configuration patch clamping) have been performed to investigate the physiological effect of HgeTx1 on Shaker B K+-channels in insect cell cultures. These recordings show that HgeTx1 reversibly blocks the Shaker B K+-channel. This blockage follows a Michaelis-Menten saturation relationship with a Kd of 52 nM.[2] However, there is no report of selectivity for or blockage of other subtypes of K+-channels.[2][4]
Mode of action
[edit]HgeTx1 has only been investigated for its effectiveness on the Shaker B K+-channel, where the toxin seems to work as a plug that blocks the pore's ion conductance. This blockage follows the functional dyad model[5][6][7] that underlies most
Toxicity
[edit]Scorpions of the family Caraboctonidae, each of which produce a cocktail of different toxins, are not considered dangerous to humans.[2]
References
[edit]- ^ Rein, J.O. "The Scorpion Files - Caraboctonidae". Retrieved 3 October 2016.
- ^ a b c d e f Schwartz, E.F.; et al. (2006). "HgeTx1, the first K+-channel specific toxin characterized from the venom of the scorpion Hadrurus gertschi Soleglad". Toxicon. 48 (8): 1046–53. doi:10.1016/j.toxicon.2006.08.009. PMID 17030052.
- ^ Tytgat, J.; et al. (1999). "A unified nomenclature for short-chain peptides isolated from scorpion venoms:
α -KTx molecular subfamilies". Trends in Pharmacological Sciences. 20 (11): 444–7. doi:10.1016/s0165-6147(99)01398-x. PMID 10542442. - ^ "Kalium: Scorpion Toxins Active on Potassium Channels". Kalium Database. Retrieved 3 October 2016.
- ^ Ménez, A. (1998). "Functional architectures of animal toxins: a clue to drug design?". Toxicon. 36 (11): 1557–72. doi:10.1016/s0041-0101(98)00148-2. PMID 9792172.
- ^ Mouhat, S.; et al. (2005). "Contribution of the functional dyad of animal toxins acting on voltage-gated Kv1-type channels". J Pept Sci. 11 (2): 65–8. doi:10.1002/psc.630. PMID 15635666. S2CID 31444823.
- ^ Kuzmenkov, A.I.; et al. (2015). "Diversity of Potassium Channel Ligands: Focus on Scorpion Toxins". Biochemistry (Moscow). 80 (13): 1764–99. doi:10.1134/S0006297915130118. PMID 26878580. S2CID 9882450.