Tau is one of the major microtubule-associated proteins in neurons. Its main role is to stabilize microtubules, supporting cytoskeletal organization, and axonal transport. Tau may undergo pathological modifications and become hyperphosphorylated. This causes the protein to accumulate into toxic assemblies that collectively lead to neurodegeneration. In Alzheimer's disease, tau proteins change shape and organize themselves into structures called neurofibrillary tangles. The tangles disrupt the transport system and are toxic to cells. Targeting tau with immunotherapies is currently the most common approach taken with Alzheimer’s disease.

Hyperphosphorylation at amino acids Ser³⁹⁶ and Ser⁴⁰⁴ has received particular attention for therapeutic targeting because of its prominence and stability in diseased tissue. This study presented the antigen-binding fragment (Fab)/epitope complex structures of three different monoclonal antibodies that target the phosphorylated Ser⁴⁰⁴ tau epitope region. The dataset contains the atomic coordinates and structure factors of Apo Fab structure of mouse monoclonal antibody 8B2, Fab/epitope complex of mouse monoclonal antibody 8B2, Fab/epitope complex of human chimeric monoclonal antibody h4E6, and Fab/epitope complex of mouse monoclonal antibody 6B2.