Ctri9577

[1] The name of the toxin derives from the first letter of the genus of Chaerilus (C), species (tri), and the clone number in the cDNA library (9577).

[1] Other scorpion toxins specific for K+ channels (KTx) commonly form a CSα/β (cysteine-stabilized α-helix-β-sheet) fold.

[1] [4] In this motif, an α-helix is connected to two or three antiparallel β-sheets and stabilized with disulfide bridges.

The predicted secondary structure of Ctri9577 is based on the typical fold of other scorpion KTxs; it consists of an α-helix connected to three antiparallel β-sheets, which is stabilized with three disulfide bridges (see figure 1).

[1][2] The blocking of the delayed rectifier Kv1.3 is expected to slow down the repolarization phase of the action potential.

Predicted secondary structure of Ctri9577. Ctri9577 contains two alpha-helices (pink), connected to three anti-parallel beta-sheets (yellow), and loops (green). The left helix will be removed in the mature protein. Image adapted from AlphaFold. [ 3 ]