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. 2004 Dec;124(6):663–677. doi: 10.1085/jgp.200409178

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Copyright © 2004, The Rockefeller University Press

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Figure 4. — Mutations of intersubunit salt bridge. (A–D) Behavior of wild-type HCN2 (A), K472E (B), E502K (C), and K472E + E502K (D) channels. Currents in response to voltage pulses to −130 mV are shown in the absence (black) and presence of saturating cAMP (red). Diagrams to the left show attractive electrostatic interactions by solid lines and repulsive electrostatic interactions by dotted lines with wild-type residues as open symbols and mutant residues as shaded symbols. (E–H) Behavior of CNGA1_cys-free (E), R431E (F), E462R (G), and R431E + E462R (H) channels. For R431E (F), the current values for cIMP are so similar to cGMP that the two traces almost overlay. Current in response to voltage pulses to +100 mV are shown in the presence of saturating cAMP (red), cIMP (blue), and cGMP (green).