Heat shock protein 90 (Hsp90) is a molecular chaperone involved in the trafficking of proteins in the cell. Under stressful conditions, Hsp90 stabilizes its client proteins and provides protection to the cell against cellular stressors such as in cancer cells. Disruption of Hsp90 leads to client protein degradation and often cell death. As Hsp90 has been found to be either overexpressed or constitutively more active in cancer cells, inhibitors of Hsp90 may have cancer cell selectivity. The N-terminal inhibitors, geldanamycin and radiciol, were the first two described inhibitors of Hsp90, but were not clinically useful. Subsequent analogues-17 allylamino-17demethoxygeldanamycin and 17 dimethylaminoethylamino-17-demethoxygeldanamycin-were found to be more clinically appropriate and have been studied in a number of clinical trials since 1999. In addition, to the N-terminal site of Hsp90, the C-terminal site appears to be another target for inhibition of Hsp90. More recently, inhibitors of the C terminus of Hsp90 have been developed and studied in vitro with promising results.