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. Author manuscript; available in PMC: 2016 Oct 25.
Published in final edited form as: Methods Mol Biol. 2011;787:33–44. doi: 10.1007/978-1-61779-295-3_3

Figure 8.1. Model of the ATPase driven conformational cycle of Hsp90 that leads to client maturation.

Figure 8.1

In addition to client and ATP, numerous co-chaperones bind to Hsp90 and influence its chaperone activity. Many of these Hsp90 binding interactions are inter-dependent. The nucleotide-bound state of Hsp90 influences the binding of both co-chaperones and clients. Understanding how the inter-dependent and often transient binding of co-chaperones and nucleotide lead to client maturation is an active area of investigation.