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首页> 外文期刊>Neuron >Structure acquisition of the T1 domain of Kv1.3 during biogenesis.
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Structure acquisition of the T1 domain of Kv1.3 during biogenesis.

机译：生物发生过程中Kv1.3的T1结构域的结构习得。

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摘要

The T1 recognition domains of voltage-gated K(+) (Kv) channel subunits form tetramers and acquire tertiary structure while still attached to their individual ribosomes. Here we ask when and in which compartment secondary and tertiary structures are acquired. We answer this question using biogenic intermediates and recently developed folding and accessibility assays to evaluate the status of the nascent Kv peptide both inside and outside of the ribosome. A compact structure (likely helical) that corresponds to a region of helicity in the mature structure is already manifest in the nascent protein within the ribosomal tunnel. The T1 domain acquires tertiary structure only after emerging from the ribosomal exit tunnel and complete synthesis of the T1-S1 linker. These measurements of ion channel folding within the ribosomal tunnel and its exit port bear on basic principles of protein folding and pave the way for understanding the molecular basis of protein misfolding, a fundamental cause of channelopathies.
机译：电压门控的K（+）（Kv）通道亚基的T1识别域形成四聚体并获得三级结构，同时仍附着于它们各自的核糖体。在这里，我们问何时何地获得二级和三级结构。我们使用生物中间体和最近开发的折叠和可及性分析来回答这个问题，以评估核糖体内部和外部的新生Kv肽的状态。在核糖体通道内的新生蛋白质中已经显示出与成熟结构中的螺旋区相对应的紧密结构（可能是螺旋形）。仅在从核糖体出口通道出现并完全合成T1-S1接头后，T1域才获得三级结构。核糖体通道及其出口中离子通道折叠的这些测量结果基于蛋白质折叠的基本原理，为理解蛋白质错误折叠的分子基础奠定了基础，蛋白质错误折叠是通道病的根本原因。

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