Molecular modeling of scorpion toxin binding to voltage-gated K+ channels
β 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 voltageβgated 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
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 β«Ψβ¬ 37 nM), Kv1.2 (Kd β«Ψβ¬ 0.8 nM), Kv1.3 (Kd β«Ψβ¬ 150 nM) voltage-gated potassium channels, as well as on small-conductance calcium-activa