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September 5, 2025Open Access

Conformational Dynamics of the Free MAX Protein Revealed by Well-Tempered Metadynamics

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Enhanced metadynamics reveals stable structures in the MAX protein, suggesting druggable targets in oncogenic pathways.

Our findings indicate that unbound MAX can adopt stable, folded conformations that were previously considered disordered.
The well-tempered metadynamics method effectively explored MAX conformational spaces, revealing thermodynamically favorable structures.
The identified meta-stable motifs in MAX suggest potential druggable sites for targeting MAX or disrupting its interaction with MYC.
This study provides a structural framework for future efforts in structure-based drug design targeting the MYC/MAX axis.

Lu et al. (2025) studied this question.

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