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首页> 外文期刊>Nature structural biology >Voltage dependent activation of potassium channels is coupled to T1 domain structure
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Voltage dependent activation of potassium channels is coupled to T1 domain structure

机译：钾通道的电压依赖性激活与T1域结构耦合

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摘要

The T1 domain, a highly conserved cytoplasmic portion at the N-terminus of the voltage-dependent K+ channel (Kv) alpha-subunit, is responsible for driving and regulating the tetramerization of the alpha-subunits. Here we report the identification of a set of mutations in the T1 domain that alter the gating properties of the Kv channel. Two mutants produce a leftward shift in the activation curve and slow the channel closing rate while a third mutation produces a rightward shift in the activation curve and speeds the channel closing rate. We have determined the crystal structures of T1 domains containing these mutations. Both of the leftward shifting mutants produce similar conformational changes in the putative membrane facing surface of the T1 domain. These results suggest that the structure of the T1 domain in this region is tightly coupled to the channel's gating states. [References: 45]
机译：T1域是电压依赖性K +通道（Kv）α亚基N端的高度保守的胞质部分，负责驱动和调节α亚基的四聚化。在这里，我们报告了在T1域中一组突变的鉴定，这些突变改变了Kv通道的门控特性。两个突变体在激活曲线中产生左移并减慢了通道的闭合速度，而第三个突变体在激活曲线中产生了右移并加快了通道的闭合速度。我们已经确定了包含这些突变的T1域的晶体结构。两个向左移动的突变体在假定的面向T1结构域的膜表面均产生相似的构象变化。这些结果表明，该区域中T1域的结构与通道的门控状态紧密耦合。 [参考：45]

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