Cover picture: External potassium (K+) enhances K channel blockade by the permeating blocker barium (Ba2+) by trapping Ba2+ in the selectivity filter (the lock-in effect). Shown here is a structural view of Ba2+ binding in NaK2K K+ channel filter in the presence of K+. A Ba2+ ion (yellow sphere) resides at site 3 in conjunction with a K+ (green sphere) at site 1 (top), representing the locked-in configuration (see research article by Lam et al., 181–192).
- PDF Icon PDF LinkTable of Contents
- PDF Icon PDF LinkEditorial Board
Disrupted coupling of gating charge displacement to Na+ current activation for DIIS4 mutations in hypokalemic periodic paralysis
Defective coupling between gating charge displacement and channel activation may contribute to reduced muscle excitability in hypokalemic periodic paralysis.
Comparison of the kinetics and voltage dependence of gating pore current conducted by S4 gating charge mutants supports the sliding-helix model of voltage sensor function and elucidates the pathogenic mechanisms underlying periodic paralysis syndromes.
Three charged amino acids in extracellular loop 1 are involved in maintaining the outer pore architecture of CFTR
Disease-associated mutation of charged amino acids in extracellular loop 1 of CFTR may reduce chloride flow by damaging the outer pore architecture.
The conserved potassium channel filter can have distinct ion binding profiles: Structural analysis of rubidium, cesium, and barium binding in NaK2K
The ion-binding profile in NaK2K is distinct from that in KcsA, even though the selectivity filter has been conserved.