Tappan, Erin published the artcileActivation of Protein Phosphatase 1 by a Small Molecule Designed to Bind to the Enzyme’s Regulatory Site, Computed Properties of 106391-88-2, the publication is Chemistry & Biology (Cambridge, MA, United States) (2008), 15(2), 167-174, database is CAplus and MEDLINE.
The activity of protein phosphatase 1 (PP1), a serine-threonine phosphatase that participates ubiquitously in cellular signaling, is controlled by a wide variety of regulatory proteins that interact with PP1 at an allosteric regulatory site that recognizes a “loose” consensus sequence (usually designated as RVXF) found in all such regulatory proteins. Peptides containing the regulatory consensus sequence have been found to recapitulate the binding and PP1 activity modulation of the regulatory proteins, suggesting that it might be possible to design small-mol. surrogates that activate PP1 rather than inhibiting it. This prospect constitutes a largely unexplored way of controlling signaling pathways that could be functionally complementary to the much more extensively explored stratagem of kinase inhibition. Based on these principles, we have designed a microcystin analog that activates PP1.
Chemistry & Biology (Cambridge, MA, United States) published new progress about 106391-88-2. 106391-88-2 belongs to esters-buliding-blocks, auxiliary class Amine,Aliphatic hydrocarbon chain,Amide,Aldehyde, name is (R)-tert-Butyl (3-methyl-1-oxobutan-2-yl)carbamate, and the molecular formula is C10H11NO4, Computed Properties of 106391-88-2.
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