5X0S

Solution NMR structure of peptide toxin SsTx from Scolopendra subspinipes mutilans

Summary for 5X0S

• Entry DOI: 10.2210/pdb5x0s/pdb
• NMR Information: BMRB: 36047
• Descriptor: SsTx (1 entity in total)
• Functional Keywords: peptide toxin, chinese red-headed centipede, toxin
• Biological source: Scolopendra mutilans
• Total number of polymer chains: 1
• Total formula weight: 6032.96

Authors

Wu, F.,Luo, L.,Qu, D.,Zhang, L.,Tian, C.,Lai, R. (deposition date: 2017-01-23, release date: 2018-01-24, Last modification date: 2024-10-23)

Primary citation

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., 115:1646-1651, 2018

PubMed Abstract: 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 (, ∼3 g) can subdue a mouse (∼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.

PubMed: 29358396
DOI: 10.1073/pnas.1714760115

Experimental method

SOLUTION NMR