Key result
In ClC chloride channels, ion permeation is intimately coupled to fast gating via a mechanism where permeating Cl(-) competes with a glutamate carboxyl group for an anion-binding site in the pore.
Describes a mechanistic model where Cl(-) competes with a glutamate gate to explain the coupling of ion permeation with fast gating in ClC channels.
Answers are grounded in this paper and cite their sources.
Elucidates ClC gating biophysics; extends structural models while leaving cardiac translation open.
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.
Tsung‐Yu Chen (2003) conducted a review in ClC chloride channel gating. In ClC chloride channels, ion permeation is intimately coupled to fast gating via a mechanism where permeating Cl(-) competes with a glutamate carboxyl group for an anion-binding site in the pore.
Synapse has enriched 10 related papers. Consider them for comparative context: