Reuveny E, Jan Y N, Jan L Y
Department of Physiology, University of California, San Francisco 94143-0724, USA.
Biophys J. 1996 Feb;70(2):754-61. doi: 10.1016/S0006-3495(96)79615-7.
Inwardly rectifying K+ channels are highly selective for K+ ions and show strong interaction with ions in the pore. Both features are important for the physiological functions of these channels and pose intriguing mechanistic questions of ion permeation. The aspartate residue in the second putative transmembrane segment of the IRK1 inwardly rectifying K+ channel, previously implicated in inward rectification gating due to cytoplasmic Mg2+ and polyamine block, is found in this study to be crucial for the channel's ability to distinguish between K+ and Rb+ ions. Mutation of this residue also perturbs the interaction between the channel pore and the Sr2+ blocking ion. Our studies suggest that this aspartate residue contributes to a selectivity filter near the cytoplasmic end of the pore.
内向整流钾通道对钾离子具有高度选择性,并在孔道中与离子表现出强烈相互作用。这两个特性对于这些通道的生理功能都很重要,并且提出了关于离子渗透的有趣机制问题。在本研究中发现,IRK1内向整流钾通道第二个假定跨膜片段中的天冬氨酸残基,先前被认为因胞质镁离子和多胺阻断而与内向整流门控有关,对于通道区分钾离子和铷离子的能力至关重要。该残基的突变也扰乱了通道孔道与锶离子阻断剂之间的相互作用。我们的研究表明,这个天冬氨酸残基有助于在孔道胞质端附近形成一个选择性过滤器。