The interaction of spider gating modifier peptides with voltage-gated potassium channels.
Gating modifier peptides bind to ion channels and alter the gating process of these molecules. One of the most extensively studied peptides, Hanatoxin (HaTx), isolated from a Chilean tarantula, has been used to characterize the blocking properties of the voltage-gated potassium channel Kv2.1. These studies have provided some insight into the gating mechanism in Kv channels. In this review we will discuss the interaction of HaTx and related spider peptides with Kv channels illustrating the properties of the binding surface of these peptides, their membrane partitioning characteristics, and will provide a working hypothesis for how the peptides inhibit gating of Kv channels. Advanced simulation results support the concept of mutual conformational changes upon peptide binding to the S3b region of the channel which will restrict movement of S4 and compromise coupling of the gating machinery to opening of the pore.
Huang
Po-Tsang
PT
Institute of Biochemistry and Molecular Biology, College of Medicine, National Taiwan University, Taiwan.
Shiau
Yu-Shuan
YS
Lou
Kuo-Long
KL
D000818:Animals; D006801:Humans; D015640:Ion Channel Gating / Q000187:drug effects / Q000502:physiology; D010455:Peptides / Q000494:pharmacology*; D026902:Potassium Channel Blockers / Q000494:pharmacology*; D024642:Potassium Channels, Voltage-Gated / Q000187:drug effects*; D013111:Spider Venoms / Q000494:pharmacology*
D010455:Peptides; D026902:Potassium Channel Blockers; D024642:Potassium Channels, Voltage-Gated; D013111:Spider Venoms; C096469:hanatoxin