IndraLab

Statements



reach
"An initial model was obtained by docking the cAMP bound HCN1 EM structure (PDB code : 5U6P) into the density map using Chimera."

reach
"In contrast to what we observe with SthK, the CNBDs in the full-length apo HCN1 channel appear to be almost identical to those in the cAMP-bound HCN1, which are in the same ‘activated’ conformation seen in other CNBDs (Lee and MacKinnon, 2017) (Figure 4—figure supplement 2)."

reach
"This movement is overall consistent with the conformational changes between the cAMP-free and cAMP bound HCN1 structure, which also suggest a concerted rotation of the C-linker and displacement of the S6-helix in favor of channel opening."

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"This displacement likely reflects the direction of conformational changes the protein may undergo upon cAMP release, and indeed, very similar residue displacements are observed when the same force is applied on the ANM of the cAMP bound HCN1 structure."