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Article

Resolving hot spots in the C-terminal dimerization domain that determine the stability of the molecular chaperone Hsp90.

PloS one - 1 Jan 2014

Ciglia Emanuele, Vergin Janina, Reimann Sven, Smits Sander H J, Schmitt Lutz, Groth Georg, Gohlke Holger

Abstract excerpt

Human heat shock protein of 90 kDa (hHsp90) is a homodimer that has an essential role in facilitating malignant transformation at the molecular level. Inhibiting hHsp90 function is a validated approach for treating different types of tumors. Inhibiting the dimerization of hHsp90 via its C-terminal domain (CTD) should provide a novel way to therapeutically interfere with hHsp90 function. Here, we predicted hot...

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Identifiers

PMID: 24760083
DOI: 10.1371/journal.pone.0096031
PMCID: PMC3997499

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