Meiselbach H, Sticht H, Enz R (2006)
Publication Type: Journal article
Publication year: 2006
Pages Range: 49-59
Journal Issue: 13
DOI: 10.1016/j.chembiol.2005.10.009
The interplay between kinases and phosphatases represents a fundamental regulatory mechanism in biological systems. Being less numerous than kinases, phosphatases increase their diversity by the acquisition of a variety of binding partners, thereby forming a large number of holoenzymes. Proteins interacting with protein phosphatase 1 (PP1) often bind via a so-called docking motif to regulate its enzymatic activity, substrate specificity, and subcellular localization. Here, we systematically determined structural elements that mediate the binding specificity of PP1 interacting proteins, and propose a refined consensus sequence for high-affinity PP1 ligands. Applying this pattern to database searches, we predicted and experimentally confirmed several previously unknown PP1 interactors. Thus, the suggested PP1 docking motif enables a highly specific prediction of PP1 binding partners, thereby facilitating the genome-wide identification of PP1 interactors.
APA:
Meiselbach, H., Sticht, H., & Enz, R. (2006). Structural analysis of the protein phosphatase 1 docking motif: Molecular description of the binding specificity identifies new ligands. Chemistry & Biology, 13, 49-59. https://doi.org/10.1016/j.chembiol.2005.10.009
MLA:
Meiselbach, Heike, Heinrich Sticht, and Ralf Enz. "Structural analysis of the protein phosphatase 1 docking motif: Molecular description of the binding specificity identifies new ligands." Chemistry & Biology 13 (2006): 49-59.
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