Abstract
Cyclic nucleotide (cN) gated ion channels such as the SthK channel are crucial in many physiological processes. Strangely, and despite their chemical similarity, cAMP acts as an activator while cGMP as an inhibitor of the SthK channel. We combined atomic force microscopy (AFM) and molecular dynamics (MD) simulations to investigate the mechanism of cyclic nucleotide binding domain (CNBD) discrimination between cAMP and cGMP. While short contact time AFM measurements revealed similar binding strengths of cAMP and cGMP, from longer contact times results suggest that ligand detection originates from the difference in binding modes of cAMP and cGMP.
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