Quasi-Anharmonic Analysis Reveals Intermediate States in the Nuclear CO-Activator Receptor Binding Domain Ensemble.

摘要

Intrinsically disordered proteins (IDPs) play a vital role in regulating cellular processes in eukaryotic cells. Structural studies have revealed that unlike well-folded globular proteins, IDPs exist as highly dynamic ensembles even under equilibrium conditions, with diverse and constantly fluctuating secondary/tertiary structure. The ability of IDPs to adapt their binding surface to recognize various binding partners provides a novel means of regulating various cellular activities. Given the abundance of IDPs in the human genome and their involvement in neurodegenerative, cardiovascular, and amyloid-related diseases, there is tremendous interest in understanding the basic molecular mechanisms by which IDPs recognize their binding partners and facilitate their specific functions.