Fig. 7: RU486 antagonism rearranges PR-SRC3-p300 interactions.
From: Structural proteomics defines a sequential priming mechanism for the progesterone receptor
A Plotted differential crosslinks in PR-B:SRC3 experiments, comparing R5020-specific (agonist, red) and RU486-specific (antagonist, blue) crosslinks. The x-axis represents the Log2 transformed fold change values from Skyline, while the y-axis represents the -log10 transformation of the Skyline p-value output. The lines are indicative of a Log2 fold change of 1 (two-fold increase) and -log10 p-value of 1.3, corresponding to p < 0.05. Each point represents a unique crosslink with corresponding XlinkX scores represented as point size. P-values were calculated by pairwise-ratio comparisons of the transition peak areas for crosslinked peptides in Skyline using linear mixed-effects models within the MSStats group comparison node115. A Red. XlinkX view of R5020-specific crosslinks in differential PR:SRC3 experiments. A Blue. XlinkX view of RU486-specific crosslinks in differential PR:SRC3 experiments. B All validated R5020-bound crosslinks for differential PR-A:SRC3:p300 ± PRE (Left) and PR-B:SRC3:p300 ± PRE (Right) experiments. Selected crosslinks, highlighted in red, show PR: SRC3-specific crosslinks. C All validated RU486-specific crosslinks for the same experimental setup described in B. Red denotes all PR:SRC3 crosslinks detected with an XlinkX score ≥ 50. Defined domains are as follows: PR - DBD (purple) and LBD (green); SRC3 – NR-boxes (gold) and histone acetyltransferase domain (violet); p300 - bromodomain (pink), zinc finger domain (green), and NCOA2-interaction domain (yellow).
