The image depicts a molecular structure of a synthetic H C N channel chimera. The structure shows the C N B D and C-linker in relation to the transmembrane domains. The C-linker of the C N B D is positioned near the cytosolic linker connecting the transmembrane domains S 4 and S 5. The image highlights structural differences between conformations of the channel. The side view perspective shows the relative orientation of the C N B D and C-linker with respect to the transmembrane domains. The transmembrane domains are arranged around a central axis, illustrating their overall organization in different conformations.
Concerted movements in a synthetic HCN channel chimera following release of cAMP from its binding site. Morphing video on concerted movement of CNBD and C-linker relative to transmembrane domains of a synthetic HCN channel. Morphing was obtained from computational data using LRT analysis of the Kv1.2/HCN4 chimera after force application to all four cAMP-binding pockets to mimic the release of cAMP from its binding site (Weißgräber et al., 2017). For visualization of the movements of CNBD and C-linker relative to the transmembrane domains, the latter have been fixed. The side view perspective predicts that the holo-to-apo-transition elicits a rotational movement of the CNBD and the C-linker relative to the transmembrane domains. In this context, the latter undergoes a pronounced iris-like rotation around a central axis.