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. Author manuscript; available in PMC: 2017 Jan 1.
Published in final edited form as: Med Res Rev. 2015 May 25;36(1):92–118. doi: 10.1002/med.21351

Figure 1.

Figure 1

Natural product inhibitors of Hsp90. 1-4 bind Hsp90 in the N-terminal ATP-binding pocket. 5 is an allosteric modulator of Hsp90. 6-8 disrupt the interaction of Hsp90 and co-chaperones. 9-11 bind the C-terminal ATP-binding motif.