Abstract

Scorpion toxins are well-known as the largest potassium channel peptide blocker family. They have been successfully proven to be valuable molecular probes for structural research on diverse potassium channels. The potassium channel pore region, including the turret and filter regions, is the binding interface for scorpion toxins, and structural features from different potassium channels have been identified using different scorpion toxins. According to the spatial orientation of channel turrets with differential sequence lengths and identities, conformational changes and molecular surface properties, the potassium channel turrets can be divided into the following three states: open state with less hindering effects on toxin binding, half-open state or half-closed state with certain effects on toxin binding, and closed state with remarkable effects on toxin binding. In this review, we summarized the diverse structural features of potassium channels explored using scorpion toxin tools and discuss future work in the field of scorpion toxin-potassium channel interactions.

Highlights

  • Potassium channels are a diverse and ubiquitous family of membrane proteins present in both excitable and non-excitable cells

  • We review the structural and functional features of representative potassium channels dissected by the representative scorpion toxins (Figure 1)

  • Concluding Remarks and Future Directions. It is well-known that scorpion toxins constitute the largest potassium channel peptide blocker family

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Summary

Introduction

Potassium channels are a diverse and ubiquitous family of membrane proteins present in both excitable and non-excitable cells They have been known to be targets of scorpion toxins for approximately 40 years, and investigations focused on the interactions between potassium channels and scorpion toxins have provided a remarkable understanding of the structure and function of diverse potassium channels [1,2,3,4]. The high resolution potassium channel structures obtained by the X-ray crystallography or cryo-electron microscopy have verified the basic features of potassium channels, such as the selectivity filter and turret topology [5,6,7] These limited structures cannot be used to elucidate the sensitivity of potassium channels to numerous scorpion toxins due to channel structural differences, especially in the turret region.

Characterization of Potassium Channels
Characterization of the hERG Channel
Characterization of SK Channels
Characterization of the IK Channel
Characterization of the BK Channel
Concluding Remarks and Future Directions
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