Abstract
The BRCA1-associated RING domain protein 1 (BARD1) is the obligate binding partner of the tumor suppressor breast cancer type 1 susceptibility protein (BRCA1) and plays a critical role in maintaining genome integrity. BARD1 contains structured N- and C-terminal domains that mediate heterodimerization with BRCA1, recognize chromatin marks, and support DNA repair functions. About 40% of BARD1 is intrinsically disordered, particularly in the central region. This intrinsically disordered region (IDR) engages DNA and key repair proteins, including RAD51, BLM, and WRN. DNA binding through the BARD1 IDR facilitates H2A ubiquitination by the BRCA1-BARD1 complex and is essential for stimulating long-range DNA end resection during homologous recombination, underscoring its role in accurate DNA repair. Despite these insights, structural characterization of the IDR remains limited, leaving questions regarding its functional interplay with BRCA1 and other repair factors unresolved. Here, we report the backbone resonance assignments of a BARD1 IDR construct spanning residues 124–270, providing a foundation for future studies aimed at understanding how the disordered regions of BARD1 interact with various binding partners and cooperate with itself and BRCA1 to regulate genome stability.