Figure 1: Accessibility of KirBac1.1 channel pore lining residues. | Nature Communications

Figure 1: Accessibility of KirBac1.1 channel pore lining residues.

From: Structural rearrangements underlying ligand-gating in Kir channels

Figure 1

Time course (a, b) and 10 min time-point data (c, d, boxed in a, b) of Alexa-Fluor 488 C5 maleimide incorporation (F, a.u.) into cysteine-substituted KirBac1.1 mutants in the presence or absence of 10 μg ml−1 diC8–PIP2 (mean±s.e., n=3 in each case; error bars are smaller than symbol in most cases) (e) Ribbon diagram indicating accessibility of AF-488 to substituted cysteine residues. Alpha carbons of tested residues in this and subsequent figures are highlighted by spheres, with inaccessible residues coloured red, limited accessible (147 and 149) purple, and highly accessible blue.

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