A possible molecular mechanism of hanatoxin binding-modified gating in voltage-gated K+-channels.

摘要: While S4 is known as the voltage sensor in voltage-gated potassium channels, carboxyl terminus of S3 (S3C) particular interest concerning site for gating modifier toxins like hanatoxin. The thus derived helical secondary structural arrangement S3C, well its surrounding environment, has since been intensively and vigorously debated. Our previous analysis based on molecular simulation provided sufficient information to describe reasonable docking conformation further experimental designs (Lou et al., 2002. J. Mol. Recognit. 15: 175–179). However, if one only relies such information, more advanced structure–functional interpretations roles S3C may play modification behavior upon toxin binding will remain unknown. In order have better understanding details regarding this issue, we performed with sequence from hanatoxin-insensitive K+-channel, shaker, analyzed conformational changes resulting docking. Compared other functional data studies respect proximity S3–S4 linker region, suggested a significant movement drk1 but not shaker direction presumably towards S4, which was comprehended possible factor interfering translocation during presence toxin. combination discussions length linker, mechanism illustrate hanatoxin binding-modified proposed. Copyright © 2003 John Wiley & Sons, Ltd.