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. 2017 Feb 28;97(1):23–40. doi: 10.1007/s41745-016-0011-3

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© The Author(s) 2017

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

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Figure 2: — Mechanism of regulation of protein function by PP-IPs. PP-IPs modulate protein function by two mechanisms: a direct binding to proteins in which the positively charged binding pockets formed by Lys/Arg residues (shown in blue) electrostatically neutralise the high negative charge of the PP-IP molecule,125 and b protein pyrophosphorylation, which involves the non-enzymatic transfer of the β-phosphate from a PP-IP to a pre-phosphorylated Ser residue (shown in mauve) surrounded by Asp/Glu residues (shown in red).