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0  structures 6  species 0  interactions 67  sequences 1  architecture

Family: Toxin_35 (PF10530)

Summary: Toxin with inhibitor cystine knot ICK or Knottin scaffold

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This is the Wikipedia entry entitled "Spider toxin". More...

Spider toxin Edit Wikipedia article

Spider toxin
1IVA.pdb.png
Solution structure of omega-agatoxin-Aa4a from Agelenopsis aperta.[1]
Identifiers
Symbol Toxin_9
Pfam PF02819
Pfam clan CL0083
InterPro IPR004169
SCOP 1oav
SUPERFAMILY 1oav
OPM superfamily 120
OPM protein 1agg
Delta Atracotoxin
Identifiers
Symbol Atracotoxin
Pfam PF05353
InterPro IPR008017
SCOP 1qdp
SUPERFAMILY 1qdp
OPM protein 1vtx
Spider toxin CSTX family
Identifiers
Symbol Toxin_35
Pfam PF10530
InterPro IPR011142
PROSITE PDOC60029
Spider potassium channel inhibitory toxin
Identifiers
Symbol Toxin_12
Pfam PF07740
Pfam clan CL0083
InterPro IPR011696
SCOP 1d1h
SUPERFAMILY 1d1h
OPM protein 1qk6

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[edit]

References[edit]

  1. ^ 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. 
  2. ^ 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. doi:10.1016/S0969-2126(97)00301-8. PMID 9384567. 
  3. ^ 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[edit]

  • 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. 

This article incorporates text from the public domain Pfam and InterPro IPR008017


This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Toxin with inhibitor cystine knot ICK or Knottin scaffold Provide feedback

Spider toxins of the CSTX family are ion channel toxins containing an inhibitor cystine knot (ICK) structural motif or Knottin scaffold. The four disulfide bonds present in the CSTX spider toxin family are arranged in the following pattern: 1-4, 2-5, 3-8 and 6-7. CSTX-1 is the most important component of C. salei venom in terms of relative abundance and toxicity and therefore is likely to contribute significantly to the overall toxicity of the whole venom. CSTX-1 blocked rat neuronal L-type, but no other types of HVA Cav channels [3]. Interestingly, the omega-toxins from Phoneutria nigriventer venom (another South American species also belonging to the Ctenidae family) are included as they carry the same disulfide bond arrangement. suggested that CSTX-1 may interact with Cav channels. Calcium ion voltage channel heteromultimer containing an L-type pore-forming alpha1-subunit is the most probable candidate for the molecular target of CSTX-1 these toxins [3].

Literature references

  1. Kuhn-Nentwig L, Schaller J, Kampfer U, Imboden H, Malli H, Nentwig W; , Arch Insect Biochem Physiol. 2000;44:101-111.: A lysine rich C-terminal tail is directly involved in the toxicity of CSTX-1, a neurotoxic peptide from the venom of the spider Cupiennius salei. PUBMED:10897091 EPMC:10897091

  2. Schalle J, Kampfer U, Schurch S, Kuhn-Nentwig L, Haeberli S, Nentwig W; , Cell Mol Life Sci. 2001;58:1538-1545.: CSTX-9, a toxic peptide from the spider Cupiennius salei: amino acid sequence, disulphide bridge pattern and comparison with other spider toxins containing the cystine knot structure. PUBMED:11693532 EPMC:11693532

  3. Kubista H, Mafra RA, Chong Y, Nicholson GM, Beirao PS, Cruz JS, Boehm S, Nentwig W, Kuhn-Nentwig L; , Neuropharmacology. 2007;52:1650-1662.: CSTX-1, a toxin from the venom of the hunting spider Cupiennius salei, is a selective blocker of L-type calcium channels in mammalian neurons. PUBMED:17517422 EPMC:17517422


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR019553

Spider toxins of the CSTX family are ion channel toxins containing an inhibitor cystine knot (ICK) structural motif or Knottin scaffold. The four disulphide bonds present in the CSTX spider toxin family are arranged in the following pattern: 1-4, 2-5, 3-8 and 6-7. CSTX-1 is the most important component of Cupiennius salei (Wandering spider) venom in terms of relative abundance and toxicity and therefore is likely to contribute significantly to the overall toxicity of the whole venom. CSTX-1 blocked rat neuronal L-type, but no other types of HVA Cav channels [PUBMED:17517422]. Interestingly, the omega-toxins from Phoneutria nigriventer (Brazilian armed spider) venom (another South American species also belonging to the Ctenidae family) are included as they carry the same disulphide bond arrangement. suggested that CSTX-1 may interact with Cav channels. Calcium ion voltage channel heteromultimer containing an L-type pore-forming alpha1-subunit is the most probable candidate for the molecular target of CSTX-1 these toxins [PUBMED:17517422].

Domain organisation

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(6)
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Representative proteomes NCBI
(71)
Meta
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RP15
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RP55
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RP75
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Seed source: PROSITE_PS60029
Previous IDs: none
Type: Family
Author: Finn R, Coggill P
Number in seed: 6
Number in full: 67
Average length of the domain: 26.30 aa
Average identity of full alignment: 76 %
Average coverage of the sequence by the domain: 26.11 %

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HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 27.8 30.1
Noise cut-off 20.6 24.7
Model length: 23
Family (HMM) version: 4
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