E.W. Grundke, D. Henderson, et al.
Molecular Physics
An unambiguous understanding of the binding mode of human progesterone to its receptor still eludes experimental search. According to the X-ray structure of the ligand-binding domain, only one (O3) of the two keto groups at the ligand ends (O3 and O20) should play a role. This result is in conflict with chemical intuition and the results of site-directed mutagenesis experiments. Herein, we report classical molecular dynamics simulations that reveal the dynamic nature of the binding in solution, elucidate the reasons why X-ray studies failed to determine the role of O20, and clarify the effects of the mutations. The predictive power of the force field is ensured by the consistent introduction of a first-principles representation of the ligand.
E.W. Grundke, D. Henderson, et al.
Molecular Physics
S.B. Broyde, S.S. Brody
Biochemical and Biophysical Research Communications
Ubaldo E. Martinez-Outschoorn, Diana Whitaker-Menezes, et al.
Cell Cycle
Kahn Rhrissorrakrai, Filippo Utro, et al.
bioRxiv