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Updated: Feb 23, 2026

Mapping the Structure-Function Relationships of Disordered Oncogenic Transcription Factors Using Transcriptomic Analysis
Published on: June 27, 2020
Hydrophobic Collapse of the Intrinsically Disordered Transcription Factor Myc Associated Factor X
Gönül Kizilsavas1, Karin Ledolter2, Dennis Kurzbach3,4
1Max Planck Institute for Polymer Research , Ackermannweg 10, 55128 Mainz, Germany.
Abstract:
The conformational space of the proto-oncogenic transcription factor Myc associated factor X (MAX) comprises a dynamic equilibrium between a stably folded coiled-coil homodimer and an intrinsically disordered ensemble of states. We show by means of nuclear magnetic resonance spectroscopy that the intrinsically disordered ensemble samples structures that are even as compact as the folded dimer. These extremely dense, hydrophobically collapsed globules might be of importance for interconversion between different conformations of intrinsically disordered proteins.
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