PROSITE documentation PDOC60029Spider toxin CSTX family signature
Description
Spider toxins of the CSTX family are ion channel toxins containing an inhibitor cystine knot (ICK) structural motif or Knottin scaffold (see <PDOC60004>) [E1]. 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.
This family includes:
- Cupiennius salei (Wandering spider) toxin CSTX-1 and its proteolytic products CSTX-2a and CSTX-2b [1].
- Cupiennius salei (Wandering spider) CSTX-9 [2].
- Cupiennius salei (Wandering spider) CSTX-13, a neurotoxic enhancer. In contrast to CSTX-1 and CSTX-9, CSTX-13 is a two-chain peptide with two interchain and two intrachain disulfide bridges [3].
We have developed a pattern that contains the six conserved cysteines with a cysteine arrangement C-C-CC-C-C which are also found in the A chain of CSTX-13.
Expert(s) to contact by email: Last update:February 2006 / First entry.
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Technical section
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References
| 1 | Authors | Kuhn-Nentwig L. Schaller J. Kaempfer U. Imboden H. Malli H. Nentwig W. |
| Title | 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. | |
| Source | Arch. Insect Biochem. Physiol. 44:101-111(2000). | |
| PubMed ID | 10897091 | |
| DOI | 10.1002/1520-6327(200007)44:3<101::AID-ARCH1>3.0.CO;2-S |
| 2 | Authors | Schaller J. Kaempfer U. Schuerch S. Kuhn-Nentwig L. Haeberli S. Nentwig W. |
| Title | 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. | |
| Source | Cell. Mol. Life Sci. 58:1538-1545(2001). | |
| PubMed ID | 11693532 |
| 3 | Authors | Wullschleger B. Kuhn-Nentwig L. Tromp J. Kaempfer U. Schaller J. Schuerch S. Nentwig W. |
| Title | CSTX-13, a highly synergistically acting two-chain neurotoxic enhancer in the venom of the spider Cupiennius salei (Ctenidae). | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 101:11251-11256(2004). | |
| PubMed ID | 15272079 | |
| DOI | 10.1073/pnas.0402226101 |
| E1 | Title | https://bioserv.cbs.cnrs.fr |
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