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. 2021 May 4;296:100744. doi: 10.1016/j.jbc.2021.100744

Figure 3.

Figure 3

Hsp90.A, the open, apo form of the bacterial Hsp90, HptG ((33), 2ioq), with one subunit in blue and the other in gold. B, the ADP-bound version of the ER form, Grp94 ((34), 2o1u). C, the closed, AMPPNP-bound state of the constitutive form Hsc82 ((35), 2cge). The green subunits are the two copies of cochaperone p23. D, the Hsp90 complex with co factor cdc37 (green) and kinase cdk4 substrate (purple) threaded through the complex with its N and C-terminal domains on opposite sides ((17), 5fwk). The linkers to the CDC37 C-terminal and CDK4 N-terminal domains are labeled. E and F, front and back views of the loading complex, formed of an Hsp90 dimer (dark and light blue), two Hsp70s (orange), the cochaperone HOP (pink), and the glucocorticoid receptor substrate (GR; yellow; (25)).