Figure 5.
Figure 5. V457E mutation abolishes con action. (A) Bar shows BD of Construct 8. Sequence alignment of the region from helix αA through strand β2 is shown for point mutants, along with their respective mean g(30 mM cGMP)/g(3 mM cGMP) ratios. Dots in alignment indicate residues conserved between fCNGA2 and rCNGA4. Amino acids mutated in each construct are circled. (B) Dose–response relation of X-fA2 V457E activated with cGMP (down-triangles; n ≥ 3 for all points). Conductances were converted to Po using the methods of Fig. 3, fixing Po = 0.359 at 3 mM cGMP. Black curve is a Hill equation fit. Fitted parameters (±SE) are: K1/2 = 350 ± 97 µM, h = 0.78 ± 0.17, and Pmax = 0.45 ± 0.03. For comparison, gray curve shows cGMP dose–response data for X-fA2 (Young et al., 2001) as in Fig. 4 B.

V457E mutation abolishes con action. (A) Bar shows BD of Construct 8. Sequence alignment of the region from helix αA through strand β2 is shown for point mutants, along with their respective mean g(30 mM cGMP)/g(3 mM cGMP) ratios. Dots in alignment indicate residues conserved between fCNGA2 and rCNGA4. Amino acids mutated in each construct are circled. (B) Dose–response relation of X-fA2 V457E activated with cGMP (down-triangles; n ≥ 3 for all points). Conductances were converted to Po using the methods of Fig. 3, fixing Po = 0.359 at 3 mM cGMP. Black curve is a Hill equation fit. Fitted parameters (±SE) are: K1/2 = 350 ± 97 µM, h = 0.78 ± 0.17, and Pmax = 0.45 ± 0.03. For comparison, gray curve shows cGMP dose–response data for X-fA2 (Young et al., 2001) as in Fig. 4 B.

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