Fig. 7: Specific electrostatic interactions between the linker and the calmodulin footprint drive the Ca2+/CaM sensitivity.
From: A domain-swapped CaMKII conformation facilitates linker-mediated allosteric regulation

A Snapshots from the MD simulation at time 0 and 33 ns containing the domain-swapped dimer (shown in inset) and exon 18 linker region. Electrostatic interactions are shown using dashed lines in the right panel. B Distributions of distance between K301 of subunit B and position 316 of subunit A from simulations of constructs with different linkers as labeled. C Same as B except comparing K301 of subunit A and position 316 of subunit B. See also Supplementary Figs. 6–11. (D) Sequences of exon 18 mutants are shown to test the position of neutral or charged residues. Net charge and EC50 values (see E) are shown. F Sequences of exon 14 mutants are shown to test the position of neutral or charged residues. Net charge and EC50 values (see G) are shown. The net charge per residue (NCPR) graphs were plotted using CIDER server (http://157.245.85.131:8000/CIDER/). Data are shown as mean ± SD, n = 3 technical replicates. Source data are provided as a Source Data Fig. 7.