Abstract
The carboxy-terminal (CT) ahnak domain encompassing ∼1000 amino acids (aa) has been implicated in cardiac Cav1.2 current (ICaL) modulation by interaction with the intracellular Cavβ2 subunit. Here we examined the requirement of a leucine zipper in ahnak-C1 (proximal ahnak CT, ∼600 aa) as well as of a PxxP motif in ahnak-C2 (distal ahnak CT, ∼400 aa) for β2 subunit binding. In ahnak-C1, surface plasmon resonance studies defined two populations of β2 subunit attachment sites without engagement of the leucine zipper motif.
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