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首页> 外文期刊>Neuron >Structural insights into the functional interaction of KChIP1 with Shal-type K(+) channels.
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Structural insights into the functional interaction of KChIP1 with Shal-type K(+) channels.

机译：结构见解的KChIP1与Shal型K（+）通道的功能相互作用。

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摘要

Four Kv channel-interacting proteins (KChIP1 through KChIP4) interact directly with the N-terminal domain of three Shal-type voltage-gated potassium channels (Kv4.1, Kv4.2, and Kv4.3) to modulate cell surface expression and function of Kv4 channels. Here we report a 2.0 Angstrom crystal structure of the core domain of KChIP1 (KChIP1*) in complex with the N-terminal fragment of Kv4.2 (Kv4.2N30). The complex reveals a clam-shaped dimeric assembly. Four EF-hands from each KChIP1 form each shell of the clam. The N-terminal end of Kv4.2 forming an alpha helix (alpha1) and the C-terminal alpha helix (H10) of KChIP1 are enclosed nearly coaxially by these shells. As a result, the H10 of KChIP1 and alpha1 of Kv4.2 mediate interactions between these two molecules, structurally reminiscent of the interactions between calmodulin and its target peptides. Site-specific mutagenesis combined with functional characterization shows that those interactions mediated by alpha1 and H10 are essential to the modulation of Kv4.2 by KChIPs.
机译：四个Kv通道相互作用蛋白（KChIP1至KChIP4）与三个Shal型电压门控钾通道（Kv4.1，Kv4.2和Kv4.3）的N末端结构域直接相互作用，以调节细胞表面表达和功能的Kv4频道在这里，我们报告了KChIP1（KChIP1 *）核心结构域与Kv4.2（Kv4.2N30）N端片段复合的2.0埃晶体结构。该复合物显示出蛤形的二聚体装配体。每个KChIP1的四只EF手形成蛤的每个壳。这些壳几乎同轴地包围了形成KvIP1的α螺旋（alpha1）的Kv4.2的N末端和KChIP1的C末端α螺旋（H10）。结果，KChIP1的H10和Kv4.2的alpha1介导了这两个分子之间的相互作用，在结构上使人联想到钙调蛋白与其靶肽之间的相互作用。特定于站点的诱变与功能表征相结合，表明由alpha1和H10介导的那些相互作用对于KChIP调节Kv4.2至关重要。

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