Diverse Structural Features of Potassium Channels Characterized by Scorpion Toxins as Molecular Probes
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...
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| Format: | Article |
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MDPI AG
2019-05-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/24/11/2045 |
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| author | Yonghui Zhao Zongyun Chen Zhijian Cao Wenxin Li Yingliang Wu |
| author_facet | Yonghui Zhao Zongyun Chen Zhijian Cao Wenxin Li Yingliang Wu |
| author_sort | Yonghui Zhao |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-12T03:27:04Z |
| format | Article |
| id | doaj.art-e7eea353661e40018d0857b47a54027d |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-12-12T03:27:04Z |
| publishDate | 2019-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-e7eea353661e40018d0857b47a54027d2022-12-22T00:40:01ZengMDPI AGMolecules1420-30492019-05-012411204510.3390/molecules24112045molecules24112045Diverse Structural Features of Potassium Channels Characterized by Scorpion Toxins as Molecular ProbesYonghui Zhao0Zongyun Chen1Zhijian Cao2Wenxin Li3Yingliang Wu4State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, ChinaState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, ChinaState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, ChinaState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, ChinaState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, ChinaScorpion 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.https://www.mdpi.com/1420-3049/24/11/2045scorpion toxinpotassium channelchannel turretopen channel conformationhalf-open or half-closed channel conformationclosed channel conformation |
| spellingShingle | Yonghui Zhao Zongyun Chen Zhijian Cao Wenxin Li Yingliang Wu Diverse Structural Features of Potassium Channels Characterized by Scorpion Toxins as Molecular Probes Molecules scorpion toxin potassium channel channel turret open channel conformation half-open or half-closed channel conformation closed channel conformation |
| title | Diverse Structural Features of Potassium Channels Characterized by Scorpion Toxins as Molecular Probes |
| title_full | Diverse Structural Features of Potassium Channels Characterized by Scorpion Toxins as Molecular Probes |
| title_fullStr | Diverse Structural Features of Potassium Channels Characterized by Scorpion Toxins as Molecular Probes |
| title_full_unstemmed | Diverse Structural Features of Potassium Channels Characterized by Scorpion Toxins as Molecular Probes |
| title_short | Diverse Structural Features of Potassium Channels Characterized by Scorpion Toxins as Molecular Probes |
| title_sort | diverse structural features of potassium channels characterized by scorpion toxins as molecular probes |
| topic | scorpion toxin potassium channel channel turret open channel conformation half-open or half-closed channel conformation closed channel conformation |
| url | https://www.mdpi.com/1420-3049/24/11/2045 |
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