Probing the Structural Dynamics of the Unbound MAX Protein: Insights from Well-Tempered Metadynamics.

ABSTRACT: One of most relevant challenges in tumorigenesis is the association of MYC and MAX proteins, whose related cancers remain undrugged. In particular, the disordered regions shown by those oncogenes make their structural characterization and the development of new drugs a truly hard task. To address these challenges, we employed the enhanced-sampling well-tempered metadynamics method to systematically explore the conformational space of the unbound MAX protein. Our results revealed, for the first time, a well-defined and thermodynamically favorable conformation of monomeric MAX. This is a remarkable finding, as it demonstrates that regions of MAX previously considered persistently disordered are capable of adopting stable, folded structures under specific conditions. Moreover, our findings al

SUBMITTER: Lu H 

PROVIDER: S-EPMC12801308 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature