The 90 kDa heat shock protein (Hsp90) is a prominent target for anticancer drug discovery. While its N-terminal domain has been widely exploited, several lines of evidence are emerging in favor of targeting its C-terminal domain to conceive innovative drugs based on perturbation of the dimer interface. Here, we describe the application of several computational approaches useful to predict the location of the C-terminal binding site.
Exploring the binding site of C-terminal Hsp90 inhibitors / Sgobba, Miriam; Forestiero, Rosetta; Degliesposti, Gianluca; Rastelli, Giulio. - In: JOURNAL OF CHEMICAL INFORMATION AND MODELING. - ISSN 1549-9596. - STAMPA. - 50:9(2010), pp. 1522-1528. [10.1021/ci1001857]
Exploring the binding site of C-terminal Hsp90 inhibitors
SGOBBA, Miriam;FORESTIERO, ROSETTA;DEGLIESPOSTI, Gianluca;RASTELLI, Giulio
2010
Abstract
The 90 kDa heat shock protein (Hsp90) is a prominent target for anticancer drug discovery. While its N-terminal domain has been widely exploited, several lines of evidence are emerging in favor of targeting its C-terminal domain to conceive innovative drugs based on perturbation of the dimer interface. Here, we describe the application of several computational approaches useful to predict the location of the C-terminal binding site.
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