Heat shock protein 90 (Hsp90) is an ATP-dependent, ubiquitously expressed and highly abundant chaperone that aids in folding, stabilizing and degrading various other proteins, including kinases, steroid hormone receptors and transcription factors. By repeated ATP hydrolysis-coupled rounds of substrate binding and release, it helps both newly synthesized and misfolded proteins to find their native fold. Since a lot of Hsp90-dependent proteins are strongly upregulated in tumor cells, mammalian Hsp90 remains a promising target for anti-cancer drugs.

protein – small molecule interaction | chaperone | MO-P-014