Skip to main content
. Author manuscript; available in PMC: 2014 Nov 1.
Published in final edited form as: Nat Chem Biol. 2013 Sep 1;9(11):677–684. doi: 10.1038/nchembio.1335

Figure 2. Structural and computational analyses define differences in Hsp90 paralog pockets and paralog-selective chemical spaces.

Figure 2

(a) Overlay of Hsp90α- and Grp94-bound PU-H54 reveals an 80° torsional rotation about the sulfanyl linker (highlighted in red) when inserted into the Grp94-specific channel. (b) Interactions of PU-H54 bound to Grp94 showing the increased hydrophobic stabilization of the 8-aryl group (X2-Ar) when bound into Site 2. (c) Surface area (left) and conformation (right) of paralog-selective chemical spaces as generated by Macromodel/Molecular Surface. Figures were created by superimposing the favored docking pose of all of the Hsp90α (top, Type 1) and Grp94 (bottom, Type 2) inhibitors described in Supplementary Figures 1 and 2.