Figure 4: The Ca2+-bound and Ca2+-free structures are nearly identical, with the same pore diameter. | Nature Communications

Figure 4: The Ca2+-bound and Ca2+-free structures are nearly identical, with the same pore diameter.

From: An electrostatic mechanism for Ca2+-mediated regulation of gap junction channels

Figure 4

The Ca2+-bound (cyan) and Ca2+-free (orange) structures, as well as the Ca2+ ions (yellow) are coloured identically to Figs 2 and 3. (a) Side views of superimposed Ca2+-bound and Ca2+-free GJC structures. (b) Plots of distance from the centre of the extracellular gap versus pore radius for the Ca2+-bound channel (cyan line) and the Ca2+-free channel (orange line). The solid horizontal lines at ±28 Å indicate the locations of the Ca2+-binding sites within each hemichannel. (c) Overlay of the Ca2+-bound (cyan) and Ca2+-free (orange) hemichannels, viewed from the extracellular gap and shown at the level of the minimum pore diameter (∼15 Å, as measured between Nζ atoms of K41) within the hemichannel, located between K41 residues of subunits that are directly across from one another. The side chains for the K41 residues are shown as sticks. A K+ ion is shown at the centre of the hemichannel with its first (7 Å diameter) and second (12 Å diameter) hydration shells shown in dark and light blue, respectively. (d) A van der Waals surface representation of the Ca2+-free Cx26 hemichannel. The K+ ion and hydration spheres are shown as in c.

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