Crystal structure of the middle and C-terminal domains of Hsp90α labeled with a coumarin derivative reveals a potential allosteric binding site as a drug target

Peng, S.; Woodruff, J.; Pathak, P.K.; Matts, R.L.; Deng, J.

doi:10.1107/S2059798322002261

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 3
Conformational changes of the Src loop induced by MDCC binding. (a) Structural superimposition of MDCC–Hsp90αMC (magenta), yeast Hsc82 (light blue; PDB entry 2cge) and the yeast Hsc82–Aha1 complex (Hsc82, green; Aha1, cyan; PDB entry 6xlb). (b) Structural superimposition of MDCC–Hsp90αMC (magenta) and closed-state full-length human Hsp90α (gray; PDB entry 7l7j). The insets detail the Src-loop conformations, with the two Phe residues shown in stick representation.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 78| Part 5| May 2022| Pages 571-585

https://doi.org/10.1107/S2059798322002261

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