Fig. 8
From: RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex
A cartoon for the structural and functional model for R2TP. a Human R2TP. HSP90 dimers can engage with each R2TP complex with sufficient conformational flexibility to reach and act in a diversity of client proteins. Up to 3 RBDs serve to anchor 3 RPAP3 to the RUVBL1–RUVBL2 scaffold, whereas a central segment of RPAP3 helps to recruit PIH1D1. The number of RPAP3 molecules per RUVBL ring in vivo is not known, and two options are shown in the figure. A long and poorly structured link between the RBD and TPR domains in RPAP3 results in substantially conformational flexibility of the TPR regions. For simplicity, although 3 RBDs are bound to the RUVBL ring, only 2 RPAP3s are shown bound to HSP90 in the cartoon. b Yeast R2TP. Conformational adaptability of yeast R2TP is limited to the flexibility of the C-terminal tails in Hsp90. Only one Hsp90 binds each R2TP.
