The interactions of apamin and tetraethylammonium are differentially affected by single mutations in the pore mouth of small conductance calcium-activated potassium (SK) channels.

Abstract excerpt

Valine residues in the pore region of SK2 (V366) and SK3 (V520) were replaced by either an alanine or a phenylalanine to evaluate the impact on the interactions with the allosteric blocker apamin. Unlike TEA which showed high sensitivity to phenylalanine mutated channels, the binding affinity of...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Alanine
• Share to HEK293 Cells
• Share to Inhibitory Concentration 50