Comparison of permeation mechanisms in sodium-selective ion channels

• Published in: Neuroscience letters Vol. 700; pp. 3 - 8
• Main Authors: Boiteux, Céline, Flood, Emelie, Allen, Toby W.
• Format: Journal Article
• Language: English
• Published: Ireland Elsevier B.V 01.05.2019
• Subjects: Acid sensing ion channel; Acid Sensing Ion Channels - chemistry; Acid Sensing Ion Channels - physiology; Animals; Bacterial Proteins - chemistry; Bacterial Proteins - physiology; Humans; Ion Channel Gating; Ion permeation; Ion selectivity; Molecular dynamics simulation; Permeability; Protein Conformation; Voltage-gated sodium channel; Voltage-Gated Sodium Channels - chemistry; Voltage-Gated Sodium Channels - physiology; Acid sensing ion channel; Molecular dynamics simulation; Ion permeation; Voltage-gated sodium channel; Ion selectivity
• ISSN: 0304-3940; 1872-7972
• DOI: 10.1016/j.neulet.2018.05.036

Voltage-gated sodium channels are the molecular components of electrical signaling in the body, yet the molecular origins of Na+-selective transport remain obscured by diverse protein chemistries within this family of ion channels. In particular, bacterial and mammalian sodium channels are known to exhibit similar relative ion permeabilities for Na+ over K+ ions, despite their distinct signature EEEE and DEKA sequences. Atomic-level molecular dynamics simulations using high-resolution bacterial channel structures and mammalian channel models have begun to describe how these sequences lead to analogous high field strength ion binding sites that drive Na+ conduction. Similar complexes have also been identified in unrelated acid sensing ion channels involving glutamate and aspartate side chains that control their selectivity. These studies suggest the possibility of a common origin for Na+ selective binding and transport.