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The structural basis of these processes has not been resolved due to the disordered nature of the NTD, which hinders experimental analyses of its detailed conformations. Here, using extensive computational modeling, we show that AR\u2010NTD forms dynamic compact regions, which upon pQe re\u2010organize dynamically, mediated partly by direct pQ interaction with the Androgen N\u2010Terminal Signature (ANTS) motif. The altered dynamics of the NTD result in a perturbation of interdomain interactions, with potential implications for the binding of the receptor protein to its response element. Oligomeric aggregation of the dynamic misfolded NTD exposes pQe, but blocks tau\u20105 and the FQNLF motif, which could lead to aberrant receptor transcriptional activity. 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