IndraLab

Statements

3',5'-cyclic AMP binds HCN1. 9 / 9
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"Figure 1 shows the holo structure of HCN4, which is a tetrameric protein overall similar in its 3D structure to cAMP-bound HCN1 (Lee and MacKinnon, 2017)."
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"Structural comparison of CNBDs in the HCN1/cAMP complex and SKOR indicates potential clashes between cAMP and the side chain of Q482 in SKOR (Supplementary Fig. S7c), which is in consistent with the functional results."
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"However, cAMP binding to the HCN1 C-terminal tetramer was not cooperative and the affinity, as well as the associated energetics, were similar to the low affinity binding event for the HCN2 C-terminal[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"These helices, named D and E (αDE) since they follow αC of the CNBD, are visible only in the cAMP-bound state of the HCN1 channel structure (Fig. 1a) ."
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"In contrast, a recent single-molecule binding study reported that cAMP binds independently to all four subunits in both non-activated HCN1 and HCN2 channels (14)."
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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."
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"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)."
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"An initial model was obtained by docking the cAMP bound HCN1 EM structure (PDB code : 5U6P) into the density map using Chimera."
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"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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