Solution NMR structure of peptide toxin SsTx from Scolopendra subspinipes mutilansSolution NMR structure of peptide toxin SsTx from Scolopendra subspinipes mutilans

Structural highlights

5x0s is a 1 chain structure with sequence from Scolopendra subspinipes. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 20 models
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TXF1A_SCOMU

Publication Abstract from PubMed

Centipedes can subdue giant prey by using venom, which is metabolically expensive to synthesize and thus used frugally through efficiently disrupting essential physiological systems. Here, we show that a centipede (Scolopendra subspinipes mutilans, approximately 3 g) can subdue a mouse ( approximately 45 g) within 30 seconds. We found that this observation is largely due to a peptide toxin in the venom, SsTx, and further established that SsTx blocks KCNQ potassium channels to exert the lethal toxicity. We also demonstrated that a KCNQ opener, retigabine, neutralizes the toxicity of a centipede's venom. The study indicates that centipedes' venom has evolved to simultaneously disrupt cardiovascular, respiratory, muscular, and nervous systems by targeting the broadly distributed KCNQ channels, thus providing a therapeutic strategy for centipede envenomation.

Centipedes subdue giant prey by blocking KCNQ channels.,Luo L, Li B, Wang S, Wu F, Wang X, Liang P, Ombati R, Chen J, Lu X, Cui J, Lu Q, Zhang L, Zhou M, Tian C, Yang S, Lai R Proc Natl Acad Sci U S A. 2018 Jan 22. pii: 1714760115. doi:, 10.1073/pnas.1714760115. PMID:29358396[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Luo L, Li B, Wang S, Wu F, Wang X, Liang P, Ombati R, Chen J, Lu X, Cui J, Lu Q, Zhang L, Zhou M, Tian C, Yang S, Lai R. Centipedes subdue giant prey by blocking KCNQ channels. Proc Natl Acad Sci U S A. 2018 Jan 22. pii: 1714760115. doi:, 10.1073/pnas.1714760115. PMID:29358396 doi:http://dx.doi.org/10.1073/pnas.1714760115
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