Abstract
Diacylglycerol (DAG)-binding C1 domains of Protein kinase C (PKC) isoforms are prime drug targets for intervention in cancers, neurodegenerative diseases, and HIV/AIDS progression. For nearly three decades, structural characterization of C1-DAG and exogenous agonist interactions at atomic resolution has remained a “dark side” of PKC pharmacology. This is attributed to immense technical difficulties in developing optimal hydrophobic scaffolds to facilitate the crystallization of amphipathic protein-ligand complexes.
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