Figure 2: Interdomain contacts between TPR2B and DP2.
From: Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules
(a) Left: overlay of 15N-HSQC spectra for isolated TPR2B, isolated DP2 and TPR2B-DP2. Right, upper panel: chemical shift differences plotted as a function against residues. Right, bottom panel: mapping of the shifts into a model of TPR2B-DP2 generated from the isolated structures (PDB 2LLW and 3UPV) using Xplor-NIH. (b) PRE data for the interaction between TPR2B and different PROXYL labelled DP2 variants in the two-domain construct and mapping of the positions onto a model of TPR2B-DP2. The position of the spin label is indicated in green. (c) NMR/SAXS model of Sti1 TPR2A–TPR2B–DP2. The five best structures based on the fit to the experimental data of 50 calculated structures were selected and aligned to TPR2A-TPR2B (residues 262–515). The positions of the E525C spin label, chemical shift perturbations and highest PREs in TPR2B (residues coloured red) are highlighted. The TPR and DP domains are shown in blue and green, respectively. The Cα atoms of flexible residues were modelled by the program CORAL and are shown as grey spheres.
