1Y2P

Solution structure of Hstx3P

1Y2P の概要

• エントリーDOI: 10.2210/pdb1y2p/pdb
• 分子名称: Neurotoxin HsTX1 (1 entity in total)
• 機能のキーワード: hstx3p, potassium channel, toxin
• 細胞内の位置: Secreted: P59867
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3836.59

構造登録者

Mosbah, A.,Gariga, L.,Darbon, H.,Sabatier, J.M. (登録日: 2004-11-23, 公開日: 2005-11-01, 最終更新日: 2024-10-23)

主引用文献

Carrega, L.,Mosbah, A.,Ferrat, G.,Beeton, C.,Andreotti, N.,Mansuelle, P.,Darbon, H.,De Waard, M.,Sabatier, J.M.
The impact of the fourth disulfide bridge in scorpion toxins of the alpha-KTx6 subfamily
Proteins, 61:1010-1023, 2005

PubMed Abstract: Animal toxins are highly reticulated and structured polypeptides that adopt a limited number of folds. In scorpion species, the most represented fold is the alpha/beta scaffold in which an helical structure is connected to an antiparallel beta-sheet by two disulfide bridges. The intimate relationship existing between peptide reticulation and folding remains poorly understood. Here, we investigated the role of disulfide bridging on the 3D structure of HsTx1, a scorpion toxin potently active on Kv1.1 and Kv1.3 channels. This toxin folds along the classical alpha/beta scaffold but belongs to a unique family of short-chain, four disulfide-bridged toxins. Removal of the fourth disulfide bridge of HsTx1 does not affect its helical structure, whereas its two-stranded beta-sheet is altered from a twisted to a nontwisted configuration. This structural change in HsTx1 is accompanied by a marked decrease in Kv1.1 and Kv1.3 current blockage, and by alterations in the toxin to channel molecular contacts. In contrast, a similar removal of the fourth disulfide bridge of Pi1, another scorpion toxin from the same structural family, has no impact on its 3D structure, pharmacology, or channel interaction. These data highlight the importance of disulfide bridging in reaching the correct bioactive conformation of some toxins.

PubMed: 16247791
DOI: 10.1002/prot.20681

実験手法

SOLUTION NMR