Biology:Spider toxin

From HandWiki
Revision as of 01:19, 26 October 2022 by NBrushPhys (talk | contribs) (simplify)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Short description: Family of toxins produced by spiders
Spider toxin
1IVA.pdb.png
Solution structure of omega-agatoxin-Aa4a from Agelenopsis aperta.[1]
Identifiers
SymbolToxin_9
PfamPF02819
Pfam clanCL0083
InterProIPR004169
SCOP21oav / SCOPe / SUPFAM
OPM superfamily112
OPM protein1agg
Delta Atracotoxin
Identifiers
SymbolAtracotoxin
PfamPF05353
InterProIPR008017
SCOP21qdp / SCOPe / SUPFAM
OPM protein1vtx
Spider toxin CSTX family
Identifiers
SymbolToxin_35
PfamPF10530
InterProIPR011142
PROSITEPDOC60029
Spider potassium channel inhibitory toxin
Identifiers
SymbolToxin_12
PfamPF07740
Pfam clanCL0083
InterProIPR011696
SCOP21d1h / SCOPe / SUPFAM
OPM superfamily112
OPM protein1qk6

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 from the venom of the Sydney funnel-web spider 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.[4]

See also

References

  1. ↑ PDB: 1IVA​; "Structure-activity relationships for P-type calcium channel-selective omega-agatoxins". Nat. Struct. Biol. 1 (12): 853–6. December 1994. doi:10.1038/nsb1294-853. PMID 7773772. 
  2. ↑ 2.0 2.1 "The structure of versutoxin (delta-atracotoxin-Hv1) provides insights into the binding of site 3 neurotoxins to the voltage-gated sodium channel". Structure 5 (11): 1525–1535. 1997. doi:10.1016/S0969-2126(97)00301-8. PMID 9384567. 
  3. ↑ "Solution structure of hanatoxin1, a gating modifier of voltage-dependent K(+) channels: common surface features of gating modifier toxins". J. Mol. Biol. 297 (3): 771–780. 2000. doi:10.1006/jmbi.2000.3609. PMID 10731427. 
  4. ↑ InterPro: IPR013140

Further reading

  • "Three-dimensional solution structure of the calcium channel antagonist omega-agatoxin IVA: consensus molecular folding of calcium channel blockers". J. Mol. Biol. 250 (5): 659–71. July 1995. doi:10.1006/jmbi.1995.0406. PMID 7623383. 
This article incorporates text from the public domain Pfam and InterPro: IPR008017



Retrieved from "https://handwiki.org/wiki/index.php?title=Biology:Spider_toxin&oldid=2280120"