| dc.description.abstract | Mutations in BReast CAncer 1 protein (BRCA1) play a crucial role in DNA damage control such as double-strand DNA break repair mechanisms. Mutations in BRCA1 increase the chance of disrupted genetic integrity by their contributions to the development of breast cancer. BRCA1 must bind to its partner protein, Partner and Localizer to BRCA2 (PALB2), in order to properly carry out its function in the repair mechanism pathway, but its conformation once bound to PALB2 is not clear. In its active state, PALB2 is known to remain in an alpha-helical coiled-coil homodimer conformation. Through this observation, we hypothesized that the intrinsically disordered region of BRCA1 on its binding surface will undergo a conformational change into an alpha-helical form. In order to test this hypothesis, we first created a truncated BRCA1, making it 50 amino acids long, then conducted nuclear magnetic resonance experiments (NMR). Through the NMR experiments, we found that the binding interface of BRCA1 does change its conformation into a helical state, forming a coiled-coil heterodimer upon binding with PALB2. | |
