Toxins | |
Molecular Surface of JZTX-V (β-Theraphotoxin-Cj2a) Interacting with Voltage-Gated Sodium Channel Subtype NaV1.4 | |
Ji Luo2  Yiya Zhang2  Mengting Gong2  Shanshan Lu2  Yifeng Ma2  Xiongzhi Zeng1  | |
[1] The key Laboratory of Protein Chemistry and Developmental Biology of Ministry of Education, College of Life Science, Hunan Normal University, Changsha 410081, China; | |
关键词: spider toxin; voltage gated sodium channels; JZTX-V; NaV1.4; | |
DOI : 10.3390/toxins6072177 | |
来源: mdpi | |
【 摘 要 】
Voltage-gated sodium channels (VGSCs; NaV1.1–NaV1.9) have been proven to be critical in controlling the function of excitable cells, and human genetic evidence shows that aberrant function of these channels causes channelopathies, including epilepsy, arrhythmia, paralytic myotonia, and pain. The effects of peptide toxins, especially those isolated from spider venom, have shed light on the structure–function relationship of these channels. However, most of these toxins have not been analyzed in detail. In particular, the bioactive faces of these toxins have not been determined. Jingzhaotoxin (JZTX)-V (also known as β-theraphotoxin-Cj2a) is a 29-amino acid peptide toxin isolated from the venom of the spider C
【 授权许可】
CC BY
© 2014 by the authors; licensee MDPI, Basel, Switzerland.
【 预 览 】
Files | Size | Format | View |
---|---|---|---|
RO202003190023600ZK.pdf | 1601KB | download |