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首页> 外文期刊>Neuron >Interaction between extracellular Hanatoxin and the resting conformation of the voltage-sensor paddle in Kv channels.
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Interaction between extracellular Hanatoxin and the resting conformation of the voltage-sensor paddle in Kv channels.

机译：细胞外花粉毒素和Kv通道中电压传感器桨的静止构象之间的相互作用。

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摘要

In voltage-activated potassium (Kv) channels, basic residues in S4 enable the voltage-sensing domain to move in response to membrane depolarization and thereby trigger the activation gate to open. In the X-ray structure of the KvAP channel, the S4 helix is located near the intracellular boundary of the membrane where it forms a "voltage-sensor paddle" motif with the S3b helix. It has been proposed that the paddle is lipid-exposed and that it translocates through the membrane as it activates. We studied the interaction of externally applied Hanatoxin with the voltage-sensor paddle in Kv channels and show that the toxin binds tightly even at negative voltages where the paddle is resting and the channel is closed. Moreover, measurements of gating charge movement suggest that Hanatoxin interacts with and stabilizes the resting paddle. These findings point to an extracellular location for the resting conformation of the voltage-sensor paddle and constrain its transmembrane movements during activation.
机译：在电压激活的钾（Kv）通道中，S4中的碱性残基使电压感应域响应膜去极化而移动，从而触发激活门打开。在KvAP通道的X射线结构中，S4螺旋位于膜的细胞内边界附近，在此处它与S3b螺旋形成“电压传感器桨”基序。已经提出，桨板是脂质暴露的，并且在其激活时其通过膜移位。我们研究了外部施用的Hanatoxin与Kv通道中的电压传感器桨的相互作用，结果表明，即使在桨处于静止状态且通道关闭的负电压下，毒素也能紧密结合。此外，对门电荷运动的测量表明，Hanatoxin与静息桨相互作用并使其稳定。这些发现指向电压传感器桨的静止构象的细胞外位置，并限制了其在激活过程中的跨膜运动。

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