HERG potassium channel regulation by the N-terminal eag domain.
HERG potassium channel regulation by the N-terminal eag domain.
复制标题
DOI：
10.1016/j.cellsig.2012.04.004
复制
发表时间：
2012-08
影响因子：
4.8
通讯作者：
Trudeau MC
中科院分区：
文献类型：
--
作者：
Gustina AS;Trudeau MC
人ether-á-go-go相关基因（hERG，Kv11.1）钾通道在心脏兴奋性中发挥重要作用。与其他 Kv 通道一样，hERG 是由膜电压激活的；然而，与其他 Kv 通道不同，hERG 通道的关闭（失活）动力学异常缓慢。缓慢失活的机制涉及 N 端“eag 域”，其中包含 PAS (Per-Arnt-Sim) 域和短 Cap 域。在这里，我们回顾了了解 eag 结构域如何调节失活的最新进展，包括 eag 结构域的几种新的核磁共振 (NMR) 解决方案结构，以及表明 eag 结构域与 C 末端 C 连接子和环状核苷酸结合同源结构域直接相互作用的证据。
Human ether-á-go-go related gene (hERG, Kv11.1) potassium channels play a significant role in cardiac excitability. Like other Kv channels, hERG is activated by membrane voltage; however, distinct from other Kv channels, hERG channels have unusually slow kinetics of closing (deactivation). The mechanism for slow deactivation involves an N-terminal “eag domain” which comprises a PAS (Per-Arnt-Sim) domain and a short Cap domain. Here we review recent advances in understanding how the eag domain regulates deactivation, including several new Nuclear Magnetic Resonance (NMR) solution structures of the eag domain, and evidence showing that the eag domain makes a direct interaction with the C-terminal C-linker and Cyclic Nucleotide-Binding Homology Domain.