Article
Analysis of the interaction of tarantula toxin Jingzhaotoxin-III (β-TRTX-Cj1α) with the voltage sensor of Kv2.1 uncovers the molecular basis for cross-activities on Kv2.1 and Nav1.5 channels.
Biochemistry - 22 Oct 2013
Tao Huai, Chen Jin J, Xiao Yu C, Wu Yuan Y, Su Hai B, Li Dan, Wang Heng Y, Deng Mei C, Wang Mei C, Liu Zhong H, Liang Song P
Abstract excerpt
Animal venoms contain a fascinating array of divergent peptide toxins that have cross-activities on different types of voltage-gated ion channels. However, the underlying mechanism remains poorly understood. Jingzhaotoxin-III (JZTX-III), a 36-residue peptide from the tarantula Chilobrachys jingzhao, is specific for Nav1.5 and Kv2.1 channels over the majority of other ion channel subtypes. JZTX-III traps the...
Topics
- Amino Acid Sequence
- Animals
- Electrophysiology
- Female
- Ion Channel Gating
- Models, Molecular
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- NAV1.5 Voltage-Gated Sodium Channel