Fig. 4: p300 differentially alters the conformational dynamics of PR-A and PR-B within the PR:SRC3:p300 complex.
From: Structural proteomics defines a sequential priming mechanism for the progesterone receptor
A Consolidated HDX plots of PR-A showing the differential HDX-MS comparisons within the plot to the left. Changes in deuterium uptake are represented by the rainbow plot shown, where darker blues correspond to decreased differential deuterium exchange and warmer reds correspond to increases in differential deuterium exchange. Common PR domains are highlighted above consolidated data: N-terminal domain (NTD, orange), DNA-binding domain (DBD, purple), Hinge (yellow), and ligand-binding domain (LBD, teal). B AlphaFold3.0 models of PR from the AF1 to LBD (amino acids 456-933 using PR-B numbering). HDX-MS overlays represent the same experiments as the consolidated views in A. Each color represents the percent change in deuterium incorporation (Δ%D), following the scale shown at the bottom. Exchange data is representative of a full seven-timepoint differential HDX experiment with sample injection after 10, 30, 60, 300, 900, and 3600 s of deuterium exchange. Gray overlays indicate no significant changes, and black indicates peptides not detected in the HDX-MS experiment.
