Fig. 3
From: Advances in the structures, mechanisms and targeting of molecular chaperones
The PPIs between HSP molecular chaperones and co-chaperones are complex. Various types of co-chaperones and their respective binding sites on HSPs. On the basis of their function, the co-chaperones of HSP90 can be divided into three classes: HSP90 ATPase activity regulators that mainly bind with HSP90 NTD and MD, HSP90 client adapters that mainly bind with HSP90 NTD, and HSP90 chaperone cycle contributors containing TPR domains that bind with MEEVD motif of HSP90 CTD. The co-chaperones of HSP70 can be divided into three classes: including ATPase activity stimulators that bind with the HSP70 NBD, nucleotide exchange factors (NEFs) that also bind with the HSP70 NBD, and regulators containing the TPR domain that bind with the EEVD motif of the HSP70 CTD. Aside from HSP90 and HSP70, reported co-chaperones of other HSPs are very few. BAG3 reportedly interacts with sHSPs, including HSP20, HSP27 and HSP22. The best-studied co-chaperone of HSP60 is HSP10
