Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
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DOI：
10.1126/science.1116269
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发表时间：
2005-08-05
期刊：
影响因子：
56.9
通讯作者：
MacKinnon, R
中科院分区：
文献类型：
--
作者：
Long, SB;Campbell, EB;MacKinnon, R
电压依赖性钾离子通道(Kv通道)通过膜电压的改变将K+离子传导到细胞膜，从而通过调节动作电位的形状和频率来调节神经元的兴奋性。在这里，我们报道了哺乳动物Kv通道Kv1.2的晶体结构，它是Shaker K+通道家族的成员。这种结构与氧化还原酶β亚基是复杂的，这种亚基可以在哺乳动物的天然细胞环境中调节Kv通道。孔的活化门是打开的。大的侧门在毛孔和细胞质之间连通。T1结构域和β亚基的侧门和位置的静电特性与失活门控的电生理学研究以及β亚基调节K+通道的可能性是一致的。
Voltage-de pendent potassium ion (K+) channels (Kv channels) conduct K+ ions across the cell membrane in response to changes in the membrane voltage, thereby regulating neuronal excitability by modulating the shape and frequency of action potentials. Here we report the crystal structure, at a resolution of 2.9 angstroms, of a mammalian Kv channel, Kv1.2, which is a member of the Shaker K+ channel family. This structure is in complex with an oxido-reductase beta subunit of the kind that can regulate mammalian Kv channels in their native cell environment. The activation gate of the pore is open. Large side portals communicate between the pore and the cytoplasm. Electrostatic properties of the side portals and positions of the T1 domain and beta subunit are consistent with etectrophysiologicat studies of inactivation gating and with the possibility of K+ channel regulation by the beta subunit.