Fig. 4: Architecture of the GR:Hsp90:FKBP51 complex.
From: Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the glucocorticoid receptor
a, Composite cryo-EM map of the GR:Hsp90:FKBP51 complex. Hsp90A, dark blue; Hsp90B, light blue; GR, yellow; FKBP51, purple. Color scheme is maintained throughout. b, Atomic model in cartoon representation with boxes corresponding to the interfaces shown in detail in c–e. c, Interface 1 between GR (yellow) and the FKBP51 FK1 domain (purple), showing interacting side chains and hydrogen bonds (dashed pink lines). d, Interface 2 between GR (yellow) and the FKBP51 FK2 domain (purple), showing interacting side chains and hydrogen bonds (dashed pink lines). e, Interface 3 between GR (yellow) and the FKBP51 FK2–TPR linker (yellow), showing interacting side chains and hydrogen bonds (dashed pink lines). f, Equilibrium binding of 10 nM F-dex to 100 nM GR DBD–LBD with chaperones, 15 μM FKBP51 (‘51’), 15 μM FKBP52 (‘52’) or mutants (mean ± s.d.). n = 3 biologically independent samples per condition. ‘Chaperones’: 15 μM Hsp70, Hsp90, Hop, and p23 or p23Δhelix; 2 μM Ydj1 and Bag-1. Significance was evaluated using a one-way analysis of variance (F(5,12) = 404.1; P < 0.0001) with post-hoc Šídák’s test (n.s. P > 0.05; *P ≤ 0.05; **P ≤ 0.01; ***P ≤ 0.001; ****P ≤ 0.0001). P values: P(chaperones versus chaperones with p23Δhelix) <0.0001, P(chaperones versus chaperones with p23Δhelix + 51) 0.0343, P(chaperones with p23Δhelix + 51 versus chaperones with p23Δhelix + 51 L119P) <0.0001, P(chaperones with p23Δhelix + 51 versus chaperones with p23Δhelix + 52) <0.0001, P(chaperones with p23Δhelix + 52 versus chaperones with p23Δhelix + 52 P119L) <0.0001, P(chaperones with p23Δhelix + 51 P119L versus chaperones with p23Δhelix + 52 P119L) <0.0001.
