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. Author manuscript; available in PMC: 2016 Jan 1.
Published in final edited form as: Annu Rev Physiol. 2014 Oct 2;77:81–104. doi: 10.1146/annurev-physiol-021113-170358

Figure 4.

Figure 4

Regulation of PI(4,5)P2 interactions with the SK2/CaM complex by phosphorylation. (a) The putative PI(4,5)P2-binding site includes the CaM linker and the SK2 channel fragment before the CaM-binding domain. (b) Molecular dynamics simulations showing the interactions of the PI(4,5)P2 phosphates with the positively charged K77 (CaM) and K402 and K405 (SK2). (c) Phosphomimetic T79D mutation of CaM decreases the interaction between the PI(4,5)P2-binding site and the PI(4,5)P2 head group (atomic distances between interacting residues are shown in angstroms). Abbreviation: CaM, calmodulin; PI(4,5)P2, phosphatidylinositol 4,5-bisphosphate; SK2, small-conductance K+ channel subtype 2.