-
Cover Image
Cover Image
Cover picture: Modulating the gating of CFTR variants through an energetically additive mechanism. The CFTR channel is depicted as in a simple two-state transition once dimerization of its nucleotide-binding domains is prohibited by mutations. Two CFTR modulators, VX-770 (in licorice representation) and nitrate (in space-filling model), independently alter this gating equilibrium by binding at the protein–lipid and protein–water interfaces, respectively (see research article by Yeh et al., 47–60).
- PDF Icon PDF LinkTable of Contents
- PDF Icon PDF LinkEditorial Board
Generally Physiological
Meeting Summary
Review
Commentary
Article
Mechanism of activation of the prokaryotic channel ELIC by propylamine: A single-channel study
The prokaryotic ligand-gated channel ELIC opens to two open states when maximally activated by the binding of at least two agonist molecules.
Modulation of CFTR gating by permeant ions
The permeant ion nitrate modulates CFTR gating to increase its open probability through a mechanism similar to that of VX-770.
Hydrophobic interaction between contiguous residues in the S6 transmembrane segment acts as a stimuli integration node in the BK channel
Phenylalanine 380 and leucine 377 in the BK channel S6 transmembrane helix of contiguous subunits participate in a hydrophobic interaction in both the closed and open state; this interaction is important in the allosteric coupling between the Ca2+ and voltage sensors and pore domain.
