NMR-identification of the interaction between BRCA1 and the intrinsically disordered monomer of the Myc-associated factor X.

ABSTRACT: The breast cancer susceptibility 1 (BRCA1) protein plays a pivotal role in modulating the transcriptional activity of the vital intrinsically disordered transcription factor MYC. In this regard, mutations of BRCA1 and interruption of its regulatory activity are related to hereditary breast and ovarian cancer (HBOC). Interestingly, so far, MYC's main dimerization partner MAX (MYC-associated factor X) has not been found to bind BRCA1 despite a high sequence similarity between both oncoproteins. Herein, we show that a potential reason for this discrepancy is the heterogeneous conformational space of MAX, which encloses a well-documented folded coiled-coil homodimer as well as a less common intrinsically disordered monomer state-contrary to MYC, which exists mostly as intrinsically disordered

SUBMITTER: Epasto LM 

PROVIDER: S-EPMC10731500 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature