Structure of the SthK Carboxy-Terminal Region Reveals a Gating Mechanism for Cyclic Nucleotide-Modulated Ion Channels
Fig 2
The SthK-Cterm structure in complex with the agonist cAMP is in a more open conformation than in the complex with the antagonist cGMP.
a) Top down cartoon view of the SthK-Cterm structure in complex with cGMP is shown in blue b) Same view as in a) for SthK-Cterm in complex with cAMP, shown in red. The yellow spheres indicate the position where the C-linker starts and is also the site where the C-linker connects to the gate of the channel. c) Differences in monomer conformation after superposition of the cAMP-bound tetramer onto the cGMP-bound tetramer. Blue is cGMP-bound, red is cAMP-bound. d) Side view of SthK-Cterm in complex with cGMP with one subunit omitted for clarity. e) same view as in d) but for SthK-Cterm in complex with cAMP.