Interactions between a pore-blocking peptide and the voltage sensor of the sodium channel: An electrostatic approach to channel geometry

被引:82
作者
French, RJ
PrusakSochaczewski, E
Zamponi, GW
Becker, S
Kularatna, AS
Horn, R
机构
[1] MAX PLANCK INST BIOPHYS, W-6000 FRANKFURT, GERMANY
[2] THOMAS JEFFERSON UNIV, JEFFERSON MED COLL, DEPT PHYSIOL, PHILADELPHIA, PA 19107 USA
关键词
D O I
10.1016/S0896-6273(00)80058-6
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
Few experimental data illuminate the relationship between the molecular structures that mediate ion conduction through voltage-dependent ion channels and the structures responsible for sensing transmembrane voltage and controlling gating. To fill this void, we have used a strongly cationic, mutated mu-conotoxin peptide, which only partially blocks current through voltage-dependent sodium channels, to study voltage-dependent activation gating in both bound and unbound channels. When the peptide binds to the ion-conducting pore, it inhibits channel opening, necessitating stronger depolarization for channel activation. We show that this activation shift could result entirely from electrostatic inhibition of the movement of the voltage-sensing S4 charges and estimate the approximate physical distance through which the S4 charges move.
引用
收藏
页码:407 / 413
页数:7
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