Summary: Ion channel inhibitory toxin
This is the Wikipedia entry entitled "Spider toxin". More...
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Spider toxin Edit Wikipedia article
|Solution structure of omega-agatoxin-Aa4a from Agelenopsis aperta.|
|Spider toxin CSTX family|
|Spider potassium channel inhibitory toxin|
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. 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 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. See also Huwentoxin-1 IPR013140.
 See also
- PDB 1IVA; Reily MD, Holub KE, Gray WR, Norris TM, Adams ME (December 1994). "Structure-activity relationships for P-type calcium channel-selective omega-agatoxins". Nat. Struct. Biol. 1 (12): 853–6. doi:10.1038/nsb1294-853. PMID 7773772.
- 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. doi:10.1016/S0969-2126(97)00301-8. 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. doi:10.1006/jmbi.2000.3609. PMID 10731427.
 Further reading
- Kim JI, Konishi S, Iwai H, Kohno T, Gouda H, Shimada I, Sato K, Arata Y (July 1995). "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. doi:10.1006/jmbi.1995.0406. PMID 7623383.
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Ion channel inhibitory toxin Provide feedback
This is a family of potent toxins that function as ion-channel inhibitors for several different ions. Omega-Grammotoxin SIA is a VSCC antagonist that inhibits neuronal N- and P-type VSCC responses . Huwentoxin-IV, from the Chinese bird spider, is a highly potent neurotoxin that specifically inhibits the neuronal tetrodotoxin-sensitive voltage-gated sodium channel in rat dorsal root ganglion neurons . Hainantoxin-4, from the venom of spider Selenocosmia hainana, adopts an inhibitor cystine knot structural motif like huwentoin-IV, and is a potent antagonist that acts at site 1 on tetrodotoxin-sensitive (TTX-S) sodium channels . Study of the molecular nature of toxin-receptor interactions has helped elucidate the functioning of many ion-channels .
Lampe RA, Defeo PA, Davison MD, Young J, Herman JL, Spreen RC, Horn MB, Mangano TJ, Keith RA;, Mol Pharmacol. 1993;44:451-460.: Isolation and pharmacological characterization of omega-grammotoxin SIA, a novel peptide inhibitor of neuronal voltage-sensitive calcium channel responses. PUBMED:8394998 EPMC:8394998
Peng K, Shu Q, Liu Z, Liang S;, J Biol Chem. 2002;277:47564-47571.: Function and solution structure of huwentoxin-IV, a potent neuronal tetrodotoxin (TTX)-sensitive sodium channel antagonist from Chinese bird spider Selenocosmia huwena. PUBMED:12228241 EPMC:12228241
Liu Z, Dai J, Chen Z, Hu W, Xiao Y, Liang S;, Cell Mol Life Sci. 2003;60:972-978.: Isolation and characterization of hainantoxin-IV, a novel antagonist of tetrodotoxin-sensitive sodium channels from the Chinese bird spider Selenocosmia hainana. PUBMED:12827284 EPMC:12827284
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR011696
This is a family of potent toxins that function as ion-channel inhibitors. Omega-Grammotoxin SIA is a VSCC antagonist that inhibits neuronal N- and P-type VSCC responses [PUBMED:8394998]. Huwentoxin-IV, from the Chinese bird spider, is a highly potent neurotoxin that specifically inhibits the neuronal tetrodotoxin-sensitive voltage-gated sodium channel in rat dorsal root ganglion neurons [PUBMED:12228241]. Hainantoxin-4, from the venom of spider Selenocosmia hainana, adopts an inhibitor cystine knot structural motif like huwentoin-IV, and is a potent antagonist that acts at site 1 on tetrodotoxin-sensitive (TTX-S) sodium channels [PUBMED:12827284]. Study of the molecular nature of toxin-receptor interactions has helped elucidate the functioning of many ion-channels [PUBMED:20189991].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||extracellular region (GO:0005576)|
|Molecular function||ion channel inhibitor activity (GO:0008200)|
|Biological process||pathogenesis (GO:0009405)|
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Curation and family details
|Seed source:||Pfam-B_20319 (release 14.0)|
|Author:||Bateman A, Finn RD|
|Number in seed:||31|
|Number in full:||254|
|Average length of the domain:||30.60 aa|
|Average identity of full alignment:||39 %|
|Average coverage of the sequence by the domain:||40.83 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||7|
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