Tau domain located in the N-terminal region encompassing residues 2-18. It activates phosphatase PP1 which dephosphorylates Ser9 in GSK3Beta and leads to its activation. In normal tau, both NTD and CTD are folded back in proximity to each other forming a 'paper-clip' conformation, which masks the PAD. Phosphorylation in the AT8 epitope, disrupts this normal conformational state, exposing the PAD by moving away the terminal domains.