Secondary structure formation of a transmembrane segment in Kv channels
Secondary structure formation of a transmembrane segment in Kv channels
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DOI：
10.1021/bi050372q
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发表时间：
2005-06-14
期刊：
影响因子：
2.9
通讯作者：
Deutsch, C
中科院分区：
文献类型：
--
作者：
Lu, JL;Deutsch, C
完整的电压门控钾 (Kv) 通道中的跨膜片段是螺旋形的，为了确定这种螺旋性是否可以首先在核糖体通道内显现，我们生成了 Kv1.3 的生物肽中间体，并使用聚乙二醇化 (PEG-MAL) 和钙调制 (CaM-MAL) 对半胱氨酸扫描的 S6 跨膜片段进行质量标记。供参考。我们创建了一种延伸肽，用作核糖核酸隧道的“分子卷尺”，并确定该隧道的功能长度为 99-112 埃。我们证明 S6 片段在核糖体隧道内形成紧凑的结构，并且 S6 的 N 端一半比 S6 的 C 端一半更紧凑。这些结果与离子通道生物发生过程中最早的折叠事件有关。
Transmembrane segments in the intact voltage-gated potassium (Kv) channel are helical, To ascertain whether this helicity could first be manifested inside the ribosomal tunnel, we generated biogenic peptide intermediates of Kv1.3 and mass-tagged the cysteine-scanned S6 trans membrane segment using pegylation (PEG-MAL) and calmodulation (CaM-MAL). For reference. we created an extended peptide that was used as a "molecular tape measure" of the ribosornal tunnel and determined that the functional length of the tunnel is 99-112 angstrom. We demonstrate that the S6 segment forms a compact structure inside the ribosomal tunnel and that the N-terminal half of S6 compacts more than the C-terminal half of S6. These results bear on the earliest folding events during biogenesis of ion channels.