钾离子通过大电导的Ca2 +活化钾通道的渗透机理。,ACS Chemical Neuroscience

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钾离子通过大电导的Ca2 +活化钾通道的渗透机理。
ACS Chemical Neuroscience ( IF 4.1 ) Pub Date : 2019-07-01 , DOI: 10.1021/acschemneuro.9b00215
Jingkang Guo ₁ , Zhiyong Tan ₂ , Yonghua Ji _{1,

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Affiliation

钾离子（K +）通过大电导Ca2 +活化钾（Slo1）通道的选择性过滤器（SF）的渗透仍然是一个值得研究的有趣问题。尽管已经揭示了K +进入SF的方式，但是K +通过SF的机制仍然不清楚。在本研究中，通过化学计算和数据挖掘，基于来自加州Ap的Slo1的分子结构，研究了通过SF的K +渗透模式。使用Discovery Studio软件研究了键构型和SF内部K +的自由能。结果表明，为了适应不断增加的能量水平并耐受更多的K +，SF的4个对称亚基只能在垂直于中心轴的一个方向上移动。此外，通常使用K + s和SF之间的两个化学键构型，包括低自由能下的螯合构型和高自由能条件下的复杂构型。此外，SF中多个K +的键结构的三个模式用于适应SF的能量变化，并且每个模式都由一个或两个子构象组成。这些发现可能是由于Slo1蛋白质功能的进化优化所致。Slo1通道的比电导和电压门控可以用当前研究中发现的K +的渗透机理来重新解释。K + s通过SF的渗透机制可用于了解各种毒素与Slo1通道之间的相互作用，

"点击查看英文标题和摘要"

Permeation Mechanism of Potassium Ions through the Large Conductance Ca2+-Activated Potassium Channel.

The permeation of the potassium ion (K+) through the selectivity filter (SF) of the large conductance Ca2+-activated potassium (Slo1) channel remains an interesting question to study. Although the mode of K+ entering and leaving the SF has been revealed, the mechanism of K+ passing through the SF is still not clear. In the present study, the pattern of K+ permeation through the SF is investigated by chemical computation and data mining based on the molecular structure of Slo1 from Aplysia californica. Both bond configurations and the free energy of K+s inside the SF was studied using Discovery Studio software. The results suggested that, to accommodate increasing energy levels and to tolerate more K+s, 4-fold symmetric subunits of SF can only move at one direction that is perpendicular to the center axis. In addition, two configurations of chemical bonds between K+s and the SF are usually employed including the chelate configuration under low free energy and the complex configuration under high free energy conditions. Moreover, three patterns of bond configurations for multiple K+s within the SF are used to accommodate the energetic changes of the SF, and each pattern is composed of one or two subconformations. These findings likely resulted from the evolutionary optimization of the protein function of Slo1. The specific conductance and the voltage-gating of the Slo1 channel can be reinterpreted with the permeation mechanism of K+s found in the current study. The permeation mechanism of K+s through the SF can be used to understand the interaction between various toxins and the Slo1 channel, and can be employed to develop new drugs targeting relevant ion channels.

更新日期：2019-06-18

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