Cover picture: Extracellular view of μ-conotoxin GIIIA binding in the outer pore of the Nav1 channel. Dark green, red, light green, orange, and cyan dots show, respectively, centers of the charged moieties in key basic residues K9, K11, R13, K16, and R19. The flexible side chains establish various specific contacts with the channel acidic residues, whereas the toxin backbone (orange rod) preserves its position and orientation (see research article by Korkosh et al., 231–244).
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Voltage dependence of permeation enhances Ca2+ influx through CaV2.2 channels relative to that of other ions at depolarized voltages.
C-type inactivation in K+ channels is enhanced by external Ca2+ or La3+, consistent with a mechanism which involves dilation of the outer pore.
Folding similarity of the outer pore region in prokaryotic and eukaryotic sodium channels revealed by docking of conotoxins GIIIA, PIIIA, and KIIIA in a NavAb-based model of Nav1.4
Analyses of toxin binding to a homology model of Nav1.4 indicate similar folding of the outer pore region in eukaryotic and prokaryotic sodium channels.
The selectivity of acid-sensing ion channels to cations depends on interactions with binding sites both within the pore and in the outer vestibule.
Fluc channels protect bacteria from accumulating F− in acidic environments.
Differences in the regulation of RyR2 from human, sheep, and rat by Ca2+ and Mg2+ in the cytoplasm and in the lumen of the sarcoplasmic reticulum
Cardiac ryanodine receptors (RyR2) from humans, rats, and sheep show differential sensitivity to calcium and magnesium, with regulation of human RyR2 resembling that of sheep more than that of rat.