Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin.

Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through the CaM-binding domain (CaMBD), which is located in an intracellular region ...
of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM. Here we report the 1.60 A crystal structure of the SK channel CaMBD/Ca2+/CaM complex. The CaMBD forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other. As only the CaM N-lobe has bound Ca2+, the structure provides a view of both calcium-dependent and -independent CaM/protein interactions. Together with biochemical data, the structure suggests a possible gating mechanism for the SK channel.
Mesh Terms:
Animals, Calmodulin, Crystallography, X-Ray, Ion Channel Gating, Models, Molecular, Potassium Channels, Potassium Channels, Calcium-Activated, Protein Binding, Protein Conformation, Protein Structure, Tertiary, Rats, Small-Conductance Calcium-Activated Potassium Channels
Nature
Date: Apr. 26, 2001
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