Kleyman T R, Sheng S, Kosari F, Kieber-Emmons T
Department of Medicine, University of Pennsylvania and VA Medical Center, Philadelphia, USA.
Semin Nephrol. 1999 Nov;19(6):524-32.
Amiloride is a prototypic inhibitor of epithelial sodium channels. Rapid progress has been made in our understanding of the structure of the sodium channel and related cation-selective channels. This work, coupled with experiments examining how selected sodium channel mutations affect amiloride binding, provides critical clues towards defining sites within the channel that bind amiloride. Residues within the channel pore and within its extracellular domain participate in amiloride binding. These results suggest that sites that interact with amiloride within the channel's extracellular domain may be in close proximity to residues within the channel's pore.
氨氯吡咪是上皮钠通道的典型抑制剂。我们对钠通道及相关阳离子选择性通道的结构的理解取得了快速进展。这项工作，再加上研究特定钠通道突变如何影响氨氯吡咪结合的实验，为确定通道内与氨氯吡咪结合的位点提供了关键线索。通道孔及其细胞外结构域内的残基参与氨氯吡咪结合。这些结果表明，通道细胞外结构域内与氨氯吡咪相互作用的位点可能与通道孔内的残基紧密相邻。
