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Hsp90 / Hsp70 chaperones interaction mediated by co-chaperone STI1

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Diana Matias

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Description: TPR2A and TPR2B domains of STI1 bind to the C-terminal of Hsp90, while the TRP1 domain physically interacts with Hsp70, bringing both together on a ternary Hsp90-STI1-Hsp70 complex and facilitating the transferring process of client proteins. This process is modulated by the presence of other co-chaperones, such as Aha1, Cpr6, Sba1 and Cdc37, which interfere in the structural conformation of Hsp90 and modify its ATPase activity.

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What does the Hsp90 / Hsp70 chaperones interaction mediated by co-chaperone STI1 template show?

TPR2A and TPR2B domains of STI1 bind to the C-terminal of Hsp90, while the TRP1 domain physically interacts with Hsp70, bringing both together on a ternary Hsp90-STI1-Hsp70 complex and facilitating the transferring process of client proteins. This process is modulated by the presence of other co-chaperones, such as Aha1, Cpr6, Sba1 and Cdc37, which interfere in the structural conformation of Hsp90 and modify its ATPase activity.

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