calcium-activated calmodulin-binding potassium channel alpha subunit

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A calcium-activated potassium channel protein that has amino- and carboxyl-terminal intracellular domains separated by a domain containing six transmembrane helices (S1-S6) in which the last two helices (S5 and S6) flank a loop, called the pore loop, which determines ion selectivity. They are subunits of the small conductance calcium-activated channels. SK channels are independent of voltage and gated solely by intracellular calcium. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the calcium-binding protein calmodulin. Calmodulin binds to the SK channel through the Calmodulin binding domain (Pfam:PF02888), which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when calcium binds the EF hands in the N-lobe of calmodulin. These channels play a crucial role in hyperpolarizing the membrane potential of excitable and nonexcitable cells. [ ]

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