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Protein kinase C (PKC) is a family of enzymes that play crucial roles in various cellular processes. Phosphorylation of PKC at different sites can influence its activity, stability, and interaction with inhibitors. Understanding how these phosphorylation sites impact inhibitor binding is essential for developing targeted therapeutic strategies.
Active Site Inhibitors and Phosphorylation Stability:
Phosphorylation and Enzyme Activity:
Different phosphorylation sites on PKC significantly impact its interaction with inhibitors. Active site inhibitors can stabilize the phosphorylated state of PKC, preventing its dephosphorylation and down-regulation. This highlights the importance of phosphorylation in maintaining PKC activity and its potential as a target for therapeutic intervention.
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