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Figure 1

From: The cochaperone CHIP marks Hsp70- and Hsp90-bound substrates for degradation through a very flexible mechanism

Figure 1

Isolation and structural characterisation of the Hsp70:p53-TMGST complex. (a) Top, size-exclusion profile of the complex (continuous line) compared with the profiles for Hsp70 (dotted line) and p53-TMGST (broken line). Bottom, the selected fractions were analysed by SDS-PAGE and stained with Coomassie blue. (b) Three orthogonal views of the Hsp70:p53-TMGST complex 3D reconstruction. (c) The same views with docking of the chaperone Hsp70 (Hsp70NBD (pdb 5aqz; green) and Hsp70 SBD (pdb 4po2; orange)) and the substrate p53-TMGST (p53DBD (pdb 2ocj; pink) and GST (pdb 1m99; cian)). The DTSSP crosslinks in the images are described in Supplementary Fig. 2c. Only crosslinks between residues located in regions with known atomic structure are depicted in the figure. Bar, 100 Å for (b,c).

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