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首页> 外文期刊>Neuron >Atomic proximity between S4 segment and pore domain in Shaker potassium channels.
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Atomic proximity between S4 segment and pore domain in Shaker potassium channels.

机译：振动筛钾通道中S4段与孔结构域之间的原子接近度。

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摘要

A recently proposed model for voltage-dependent activation in K+ channels, largely influenced by the KvAP X-ray structure, suggests that S4 is located at the periphery of the channel and moves through the lipid bilayer upon depolarization. To investigate the physical distance between S4 and the pore domain in functional channels in a native membrane environment, we engineered pairs of cysteines, one each in S4 and the pore of Shaker channels, and identified two instances of spontaneous intersubunit disulfide bond formation, between R362C/A419C and R362C/F416C. After reduction, these cysteine pairs bound Cd2+ with high affinity, verifying that the residues are in atomic proximity. Molecular modeling based on the MthK structure revealed a single position for S4 that was consistent with our results and many other experimental constraints. The model predicts that S4 is located in the groove between pore domains from different subunits, rather than at the periphery of the protein.
机译：最近提出的K +通道中电压依赖性激活的模型受到KvAP X射线结构的很大影响，该模型表明S4位于通道的外围，并在去极化时穿过脂质双层。为了研究天然膜环境中功能通道中S4和孔结构域之间的物理距离，我们设计了半胱氨酸对，每个在S4中和摇床通道的孔中，分别确定了R362C之间两个自发的亚基二硫键形成的实例/ A419C和R362C / F416C。还原后，这些半胱氨酸对以高亲和力结合Cd2 +，验证了残基在原子附近。基于MthK结构的分子建模揭示了S4的单个位置，该位置与我们的结果和许多其他实验约束一致。该模型预测，S4位于不同亚基的孔结构域之间的凹槽中，而不是蛋白质的外围。

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