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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 5. — Mutations of intrasubunit salt bridge. (A–D) Behavior of wild-type HCN2 (A), K472E (B), D542K (C), and K472E + D542K (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), R431D (F), D502R (G), and R431D + D502R (H) channels. Current in response to voltage pulses to +100 mV are shown in the presence of saturating cAMP (red), cIMP (blue), and cGMP (green).