Abstract
Though healthy cells utilize the function of the 90 kDa heat shock protein (HSP90) to control cell growth, cell survival, and development -particularly in response to cellular stress- the activity of this protein is also beneficial to the growth and survival of cancer cells. Tanespimycin (17-AAG) is a well-characterized HSP90 inhibitor that has been shown to be cytotoxic to cancer cells. The complementary structural information gained from quantitative crosslinking with mass spectrometry (qXL-MS) and the In-Cell Fast Photochemical Oxidation of Proteins (IC-FPOP) was used to investigate the inhibition of HSP90 by 17-AAG in MCF-7 breast cancer cells.
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