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This review compiles comprehensive structure\u2013activity relationship (SAR) insights essential for medicinal chemists designing selective DYRK1A inhibitors. We detail the molecular architecture of the ATP\u2010binding pocket of DYRK1A, key regulatory residues (Lys188, Phe238, Glu239, Leu241), and structure\u2013function relationships governing inhibitor classes: ATP\u2010competitive agents, ATP\u2010non\u2010competitive inhibitors, and Proteolysis\u2010Targeting Chimeras (PROTAC) degraders with emphasis on functional group modifications and scaffold optimization strategies. Readers will gain actionable insights on binding mode predictions, potency\u2010selectivity trade\u2010offs, and prioritization of lead compounds for preclinical validation. 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