Spider toxins are a family of proteins produced by spiders which function as neurotoxins. The mechanism of many spider toxins is through blockage of calcium channels.
A remotely related group of atracotoxins operate by opening sodium channels. Delta atracotoxin produces potentially fatal neurotoxic symptoms in primates by slowing the inactivation of voltage-gated sodium channels.[2] The structure of atracotoxin comprises a core beta region containing a triple-stranded a thumb-like extension protruding from the beta region and a C-terminal helix. The beta region contains a cystine knot motif, a feature seen in other neurotoxic polypeptides[2] and other spider toxins, of the CSTX family.
Spider potassium channel inhibitory toxins is another group of spider toxins. A representative of this group is hanatoxin, a 35 amino acid peptide toxin which was isolated from Chilean rose tarantula (Grammostola rosea, syn. G. spatulata) venom. It inhibits the drk1 voltage-gated potassium channel by altering the energetics of gating.[3] See also Huwentoxin-1 IPR013140.
See also
References
- ↑ PDB: 1IVA; Lua error in package.lua at line 80: module 'strict' not found.
- ↑ 2.0 2.1 Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
Further reading
- Lua error in package.lua at line 80: module 'strict' not found.
This article incorporates text from the public domain Pfam and InterPro IPR008017
<templatestyles src="Asbox/styles.css"></templatestyles>