Fig. 7
From: The architecture of EGFR’s basal complexes reveals autoinhibition mechanisms in dimers and oligomers
Equilibrium between the aTKD and sTKD dimers. a Cartoon of the two dimer configurations of the kinase domain. Starting from the aTKD dimer, a counter clockwise rotation of the activator (blue) along its vertical axis followed by a clockwise rotation along an axis perpendicular to the plane will allow the sTKD to form. b The FLImP distribution (grey) and the distributions compiled from the FLImP measurements whose 69% CIs overlap with DIII–DIII separations = 5 nm (green), 13 nm (yellow), or >20 nm (blue) collected from cells expressing K721A-EGFR compiled from 29 FLImP measurements with CI ≤ 7 nm. The inset shows the fraction of separations consistent with each distance. Errors were assesed with bootstrap-resampling12. c Fraction of tracks where two different-colour particles labelled with Alexa 488-Affibody and CF640-Affibody spent ≥5 frames (250 ms) together within <1 pixel (denoted fraction of pairwise particle colocalisation fraction) and d distribution of the duration of these pairwise interactions (τON). Horizontal spreads separate data points (~5000) within each condition. Horizontal white lines mark the mean and SD. Coincidental colocalisation statistics were accounted for. e, f As c, d but in the presence of 10 mM MβCD. p-Values of the significance of differences between conditions are in Supplementary Fig. 20
