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. 2009 Aug;134(2):151–164. doi: 10.1085/jgp.200910240

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© 2009 Martínez-François et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jgp.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 2. — A point mutation in CNGA1's pore helix renders the channel voltage sensitive. (A) Partial crystal structure model of the Kv1.2-Kv2.1 chimeric channel (PDB 2R9R) featuring the pore helix and the selectivity filter in two diagonally opposite subunits. An oxygen in the side chain of the chimera's D375 is hydrogen-bonded to the nitrogen of W362. (B–F; Left) Macroscopic currents in 2 mM cGMP for the S350A, L351A, Y352A, S354A, and T355A mutants. Each current trace for Y352A or T355A is the average of five or three individual traces. (Right) Corresponding G-V curves (mean ± SEM; n = 4–6).