Fig. 3: SRC3 induces LBD changes to PR upon PRE addition.
From: Structural proteomics defines a sequential priming mechanism for the progesterone receptor
A Left HDX overlay (PR-A vs. PR-A:SRC3, both non-DNA bound) mapped onto AlphaFold3.0 model of the PR-A:SRC3 ternary complex with the PR homodimer highlighted. Zoomed-in sections of PR corresponding to the dimerization domains (PR-B amino acids: 855-922 and 602-618) and N-terminal domain (PR-A amino acids 1-476) highlighted with matching HDX overlays. Right. Differential HDX overlay of SRC3 vs. PR-A:SRC3 onto the best scoring PR:SRC3 apo complex with SRC3 highlighted. NR-boxes 1 and 2 (amino acids 685-689 and 738-742, respectively) zoomed-in up to show differential exchange. B Left. HDX overlay (PR-A:PRE vs. PR-A:SRC3:PRE, both DNA-bound) mapped onto AlphFold3.0 model of PR-A:SRC3:PRE ternary complex with the PR homodimer highlighted. One PR-A monomer is shown as a zoomed-in section. B Right. Differential HDX overlay of SRC3 vs. PR-A:SRC3:PRE onto the best-scoring PR:SRC3 apo complex with SRC3 highlighted. NR-boxes 1 and 2 and the p300 interaction site (amino acids 1023-1093) are highlighted to show differential exchange. Black peptide regions correspond to peptides not identified by HDX-MS. Each color represents the percent change in deuterium incorporation (Δ%D), following the scale shown at the bottom, where darker blues correspond to decreased differential deuterium exchange and warmer reds correspond to increases in differential deuterium exchange. 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 exchange time.
