Extended Data Fig. 3: Candidate residues for tuning the affinity of cAMP binding. | Nature Methods

Extended Data Fig. 3: Candidate residues for tuning the affinity of cAMP binding.

From: Sensitive genetically encoded sensors for population and subcellular imaging of cAMP in vivo

Extended Data Fig. 3

a, Crystal structure analyses of the cAMP binding site of Epac2A suggests 10 positions that potentially affect the cAMP binding affinity. b, Alignment of a portion of the CNB domain of Epac1 with those of the CNG channel CNGA2 and CNGA3. Known positions at which mutations affect the affinity of the CNG channels to their ligand are shown (asterisks).

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