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. Author manuscript; available in PMC: 2017 Mar 11.
Published in final edited form as: Biochem Mol Biol J. 2017 Jan 30;3(1):2. doi: 10.21767/2471-8084.100030

Figure 3.

Figure 3

Points of co-chaperone action on structural elements of Hsp90 essential for its ATPase activity. Cdc37p50 prevents molecular rearrangement of the lids of Hsp90. HOP may prevent lid closure and N-terminal dimerization probably by interacting with the N-terminal segments of Hsp90. Aha1 appears to interact with all the structural elements leading to a co-operative N-terminally dimerized state of Hsp90. Sba1 can stabilize Hsp90 complexes by reducing the ATPase activity of Hsp90 and it appears to interact with both the lid and N-terminal domains of Hsp90. Sba1 may also modulate the middle domain catalytic loop. Sgt1-Rar1 complex, appear to activate Hsp90 in an open state and convert it to a stable ADP-bound state.