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首页> 外文期刊>Journal of Neurophysiology >Characterization of gating and peptide block of mSlo, a cloned calcium-dependent potassium channel.
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Characterization of gating and peptide block of mSlo, a cloned calcium-dependent potassium channel.

机译：mSlo（克隆的钙依赖性钾离子通道）的门控和肽阻滞的表征。

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摘要

The 20 amino acid Shaker inactivation peptide blocks mSlo, a cloned calcium-dependent potassium channel. Changing the charge and degree of hydrophobicity of the peptide alters its blocking kinetics. A "triple mutant" mSlo channel was constructed in which three amino acids (T256, S259, and L262), equivalent to those identified as part of the peptide's receptor site in the S4-S5 cytoplasmic loop region of the Shaker channel, were mutated simultaneously to alanines. These mutations produce only limited changes in the channel's susceptibility to block by a series of peptides of varying charge and hydrophobicity but do alter channel gating. The triple mutant channel shows a significant shift in its calcium-activation curve as compared with the wild-type channel. Analysis of the corresponding single amino acid mutations shows that mutation at position L262 causes the most dramatic change in mSlo gating. These results suggest that the three amino acids mutated in the mSlo S4-S5 loop may contribute to, but arenot essential for, peptide binding. On the other hand, they do play a critical role in the channel's calcium-sensing mechanism.
机译：20个氨基酸的Shaker灭活肽可阻断mSlo（克隆的钙依赖性钾离子通道）。改变肽的电荷和疏水性程度会改变其阻断动力学。构建了一个“三重突变” mSlo通道，其中同时突变了三个氨基酸（T256，S259和L262），这些氨基酸与在摇床通道的S4-S5细胞质环区域中被识别为肽受体位点的部分相同丙氨酸。这些突变只会在通道的敏感性上产生有限的变化，从而被一系列电荷和疏水性不同的肽阻断，但确实会改变通道门控。与野生型通道相比，三突变体通道在其钙激活曲线中显示出明显的变化。对相应的单个氨基酸突变的分析表明，L262位的突变引起mSlo门控的最大变化。这些结果表明在mSlo S4-S5环中突变的三个氨基酸可能有助于但不是肽结合所必需的。另一方面，它们在通道的钙感测机制中起着至关重要的作用。

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