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首页> 外文期刊>Neuron >Architecture of a K+ channel inner pore revealed by stoichiometric covalent modification.
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Architecture of a K+ channel inner pore revealed by stoichiometric covalent modification.

机译：化学计量的共价修饰揭示了K +通道内孔的结构。

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摘要

Inwardly rectifying K+ channels bind intracellular magnesium and polyamines to generate inward rectification. We have examined the architecture of the inner pore of Kir2.1 channels by covalently attaching a constrained number (from one to four) of positively charged moieties of different sizes to the channel. Our results indicate that the inner pore is formed solely by the second transmembrane segment and is unprecedentedly wide. At a position critical for inward rectification (D172), the pore is sufficiently wide to bind three Mg2+ ions or polyamine molecules simultaneously. Single-channel recordings directly demonstrate that partially modified channels exhibit distinct subconductance levels. Such a wide inner pore may greatly facilitate ion permeation and high-affinity binding of multiple pore blockers to generate strong inward rectification.
机译：向内整流的K +通道结合细胞内镁和多胺以产生向内整流。我们已经通过将约束大小（从一到四个）的大小不同的正电荷部分共价连接到通道上，研究了Kir2.1通道内部孔的结构。我们的结果表明，内孔仅由第二个跨膜片段形成，并且空前地宽。在向内整流的关键位置（D172），孔足够宽，可以同时结合三个Mg2 +离子或多胺分子。单通道录音直接表明，部分修改的通道表现出不同的亚导水平。如此宽的内部孔隙可以极大地促进离子渗透和多种孔隙阻滞剂的高亲和力结合，从而产生强大的向内整流。

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