Key result
In ClC chloride channels, ion permeation is intimately coupled to fast gating, which depends on a negatively charged carboxyl group on a glutamate residue blocking the channel pore.
This model explains how intracellular chloride affects channel gating through competition with a glutamate gate in ClC channels.
In ClC chloride (Cl–) channels, unlike cation-selective ion channels, ion permeation is intimately coupled to fast gating. Recent research comparing the crystallographic structure of a bacterial ClC channel with functional studies of a Torpedo ClC channel suggests that gating depends on the negatively charged carboxyl group on a glutamate residue, which blocks the channel pore. In this model, the permeating Cl– competes with the carboxyl group for an anion-binding site in the channel pore. This model of Cl– competition with a glutamate gate helps explain the effect of intracellular Cl– on channel gating; the mechanism underlying the effects of extracellular Cl–, however, remains to be determined, as does the nature of the Cl– channel slow gate.
No takes yet. Share an insight, caveat, or question.
T.-Y. Chen (2003) conducted a review in ClC chloride channel function. In ClC chloride channels, ion permeation is intimately coupled to fast gating, which depends on a negatively charged carboxyl group on a glutamate residue blocking the channel pore.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: