Harris C, Fliegel L
Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
Int J Mol Med. 1999 Mar;3(3):315-21. doi: 10.3892/ijmm.3.3.315.
Amiloride and its derivatives are important tools for studying NHE-1, the ubiquitous isoform of the sodium/hydrogen exchanger protein family. Three residues in putative transmembrane domains IV and IX have been implicated in amiloride binding and several models of the proposed amiloride-binding site have been reported. Though it has been shown that sodium ions and amiloride molecules interact at unique regions of the NHE-1 protein, physiological experiments reveal a competitive relationship between the two under some circumstances. The two binding sites are thus on closely related but distinct regions on the protein.
氨氯吡咪及其衍生物是研究钠/氢交换蛋白家族中普遍存在的异构体NHE-1的重要工具。推测的跨膜结构域IV和IX中的三个残基与氨氯吡咪结合有关，并且已经报道了几种氨氯吡咪结合位点的模型。虽然已经表明钠离子和氨氯吡咪分子在NHE-1蛋白的独特区域相互作用，但生理学实验揭示了在某些情况下两者之间的竞争关系。因此，这两个结合位点位于蛋白质上密切相关但不同的区域。
