Crystal Structure of the Human Two-Pore Domain Potassium Channel K2P1
Crystal Structure of the Human Two-Pore Domain Potassium Channel K2P1
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DOI：
10.1126/science.1213274
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发表时间：
2012-01-27
期刊：
影响因子：
56.9
通讯作者：
Long, Stephen B.
中科院分区：
文献类型：
--
作者：
Miller, Alexandria N.;Long, Stephen B.
双孔结构域钾离子通道（K2P通道）控制真核细胞的负静息电位，并通过传导K+离子穿过质膜来调节细胞的兴奋性。在这里，我们展示了人类K2P通道K2P1 （TWIK-1）的3.4埃分辨率晶体结构。与其他K+通道结构不同，K2P1是二聚体。位于选择性过滤器上方的胞外帽结构域形成离子通道，其中K+离子流过侧门户。跨膜区域内的开口使孔暴露于脂质双分子层，并充满可归因于烷基链的电子密度。界面螺旋在结构上似乎可以影响门控。该结构为进一步研究不同刺激对K2P通道的调节机制奠定了基础。
Two-pore domain potassium (K+) channels (K2P channels) control the negative resting potential of eukaryotic cells and regulate cell excitability by conducting K+ ions across the plasma membrane. Here, we present the 3.4 angstrom resolution crystal structure of a human K2P channel, K2P1 (TWIK-1). Unlike other K+ channel structures, K2P1 is dimeric. An extracellular cap domain located above the selectivity filter forms an ion pathway in which K+ ions flow through side portals. Openings within the transmembrane region expose the pore to the lipid bilayer and are filled with electron density attributable to alkyl chains. An interfacial helix appears structurally poised to affect gating. The structure lays a foundation to further investigate how K2P channels are regulated by diverse stimuli.