Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment
Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment
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DOI：
10.1038/nature06265
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发表时间：
2007-11-15
期刊：
影响因子：
64.8
通讯作者：
MacKinnon, Roderick
中科院分区：
文献类型：
--
作者：
Long, Stephen B.;Tao, Xiao;MacKinnon, Roderick
电压依赖性K+(Kv)通道使神经元和肌肉的动作电位重新极化。这种类型的通道通过被称为电压传感器的蛋白质结构域直接由膜电压控制，电压传感器是读取膜电压并调节孔洞的分子电压计。在这里，我们描述了一个嵌合体电压依赖的K+通道的结构，我们称之为‘桨-嵌合体通道’，其中电压传感器桨已经从Kv2.1转移到Kv1.2。在与脂类的复合体中结晶，在2.4埃分辨率下的完整结构揭示了嵌入在膜状排列的脂类分子中的孔和电压传感器。详细的结构，可以直接与大量的功能数据进行比较，解释了膜内的电荷稳定，并提出了电压传感器移动和孔门的机制。
Voltage-dependent K+ (Kv) channels repolarize the action potential in neurons and muscle. This type of channel is gated directly by membrane voltage through protein domains known as voltage sensors, which are molecular voltmeters that read the membrane voltage and regulate the pore. Here we describe the structure of a chimaeric voltage-dependent K+ channel, which we call the 'paddle-chimaera channel', in which the voltage-sensor paddle has been transferred from Kv2.1 to Kv1.2. Crystallized in complex with lipids, the complete structure at 2.4 angstrom resolution reveals the pore and voltage sensors embedded in a membrane-like arrangement of lipid molecules. The detailed structure, which can be compared directly to a large body of functional data, explains charge stabilization within the membrane and suggests a mechanism for voltage-sensor movements and pore gating.