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. 2018 Feb 1;23(4):467–482. doi: 10.1007/s12192-018-0877-2

Fig. 2.

Fig. 2

General scheme of the domain structure of Hsp90 and of the target domains of the main classes of Hsp90 inhibitors. ADP and ATP illustrate the importance of the N-terminal domain for ATP binding and hydrolysis; M and C, middle and C-terminal domains; MEEVD, very C-terminal pentapeptide (hallmark of cytosolic Hsp90 isoforms) and binding site for most of the co-chaperones containing tetratricopeptide repeats