Spider toxin
From Wikipedia, the free encyclopedia
Spider toxin | ||
---|---|---|
Identifiers | ||
Symbol | Toxin_9 | |
Pfam | PF02819 | |
InterPro | IPR004169 | |
SCOP | 1oav | |
OPM family | 120 | |
OPM protein | 1agg | |
Available PDB structures:
1iva :4-48 1oaw :4-48 1oav :4-48 1agg :39-83 1omb :39-73 1oma :39-83 |
Delta Atracotoxin | ||
---|---|---|
Identifiers | ||
Symbol | Atracotoxin | |
Pfam | PF05353 | |
InterPro | IPR008017 | |
SCOP | 1qdp | |
OPM protein | 1vtx | |
Available PDB structures: |
Spider toxin CSTX family | |
---|---|
Identifiers | |
Symbol | SPIDER_CSTX |
InterPro | IPR011142 |
PROSITE | PDOC60029 |
Spider potassium channel inhibitory toxin | ||
---|---|---|
Identifiers | ||
Symbol | Toxin_12 | |
Pfam | PF07740 | |
InterPro | IPR011696 | |
SCOP | 1d1h | |
OPM protein | 1qk6 | |
Available PDB structures:
1qk6A:49-79 1nixA:1-31 1mb6A:53-85 1rygA:1-33 1niyA:1-33 1ryvA:1-33 1emxA:2-28 1qk7A:50-77 1tykA:47-78 1d1hA:1-30 1la4A:1-30 1kozA:1-32 |
Spider neurotoxins are a family of proteins that usually work as calcium ion channel inhibitors.
A remotely related group of atratoxins operate by opening sodium channels. Delta atracotoxin produces potentially fatal neurotoxic symptoms in primates by slowing the inactivation of voltage-gated sodium channels[1]. 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[1] 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. That is a 35 amino acid peptide toxin which was isolated from Chilean tarantula (Grammostola spatulata) venom. It inhibits the drk1 voltage-gated potassium channel not by blocking the pore, but by altering the energetics of gating[2]. See also Huwentoxin-1 IPR013140.
[edit] References
- ^ a b Mackay JP, King GF, Fletcher JI, Chapman BE, Howden ME (1997). "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. PMID 9384567.
- ^ Shimada I, Sato K, Takahashi H, Kim JI, Min HJ, Swartz KJ (2000). "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. PMID 10731427.
[edit] Further reading
- Three-dimensional solution structure of the calcium channel antagonist omega-agatoxin IVA: consensus molecular folding of calcium channel blockers. Kim JI, Konishi S, Iwai H, Kohno T, Gouda H, Shimada I, Sato K, Arata Y; J Mol Biol 1995;250:659-671. PubMed
This article includes text from the public domain Pfam and InterPro IPR008017