1WQD

An unusual fold for potassium channel blockers: NMR structure of three toxins from the scorpion Opisthacanthus madagascariensis

1WQD の概要

• エントリーDOI: 10.2210/pdb1wqd/pdb
• 関連するPDBエントリー: 1WQC 1WQE
• 分子名称: OmTx2 (1 entity in total)
• 機能のキーワード: toxin
• 由来する生物種: Opisthacanthus madagascariensis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3155.51

構造登録者

Chagot, B.,Pimentel, C.,Dai, L.,Pil, J.,Tytgat, J.,Nakajima, T.,Corzo, G.,Darbon, H.,Ferrat, G. (登録日: 2004-09-28, 公開日: 2005-01-18, 最終更新日: 2022-03-02)

主引用文献

Chagot, B.,Pimentel, C.,Dai, L.,Pil, J.,Tytgat, J.,Nakajima, T.,Corzo, G.,Darbon, H.,Ferrat, G.
An unusual fold for potassium channel blockers: NMR structure of three toxins from the scorpion Opisthacanthus madagascariensis
Biochem.J., 388:263-271, 2005

PubMed Abstract: The Om-toxins are short peptides (23-27 amino acids) purified from the venom of the scorpion Opisthacanthus madagascariensis. Their pharmacological targets are thought to be potassium channels. Like Csalpha/beta (cystine-stabilized alpha/beta) toxins, the Om-toxins alter the electrophysiological properties of these channels; however, they do not share any sequence similarity with other scorpion toxins. We herein demonstrate by electrophysiological experiments that Om-toxins decrease the amplitude of the K+ current of the rat channels Kv1.1 and Kv1.2, as well as human Kv1.3. We also determine the solution structure of three of the toxins by use of two-dimensional proton NMR techniques followed by distance geometry and molecular dynamics. The structures of these three peptides display an uncommon fold for ion-channel blockers, Csalpha/alpha (cystine-stabilized alpha-helix-loop-helix), i.e. two alpha-helices connected by a loop and stabilized by two disulphide bridges. We compare the structures obtained and the dipole moments resulting from the electrostatic anisotropy of these peptides with those of the only other toxin known to share the same fold, namely kappa-hefutoxin1.

PubMed: 15631621
DOI: 10.1042/BJ20041705

実験手法

SOLUTION NMR