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Molecular modeling of scorpion toxin binding to voltage-gated K+ channels

✍ Scribed by Gregory M. Lipkind; Harry A. Fozzard


Book ID
110355748
Publisher
Springer
Year
1999
Tongue
English
Weight
95 KB
Volume
15/16
Category
Article
ISSN
0928-2866

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## Abstract The carboxyl terminus of S3 segment (S3~C~) in voltage‐gated potassium channels was proposed to bear the binding site for gating modifier toxins like Hanatoxin and a helical secondary structural arrangement was suggested. Due to the lack of complete structure in high resolution for such

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Maurotoxin (MTX), purified from the scorpionid Scorpio maurus is a potent ligand for potassium channels. It shows a broad specificity as being active on Kv1.1 (Kd ‫؍‬ 37 nM), Kv1.2 (Kd ‫؍‬ 0.8 nM), Kv1.3 (Kd ‫؍‬ 150 nM) voltage-gated potassium channels, as well as on small-conductance calcium-activa