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Target intelligence / Profile preview
Heat Shock Protein 90 (Hsp90)
- Target
- Hsp90
- Molecular classification
- Molecular chaperone, Protein
01
Overview
Heat shock protein 90 (Hsp90) is a highly conserved and abundant molecular chaperone that plays a central role in maintaining cellular proteostasis by assisting the folding, stabilization, activation, and degradation of a wide array of client proteins. It is especially important under stress conditions but also functions under normal physiological states. As a chaperone for numerous oncogenic and pro-survival client proteins, it's a significant target for cancer therapy. It's implicated in neurodegenerative diseases and viral/bacterial infection cycles as well.
- Other names
- HSP90αHSP90βGRP94TRAP1hsp90aa1hsp90ab1hspc4trap1
02
Mechanism of action
ATP-dependent conformational cycling; binds and stabilizes client proteins; inhibition disrupts client protein function.
03
Biological functions
Protein foldingProtein refoldingProtein degradationCell cycle regulationApoptosis regulationSignal transductionProteome integrity maintenanceProtein stabilization
04
Disease associations
CancerNeurodegenerative diseaseViral infectionBacterial infection
05
Safety considerations
Off-target effects due to broad client protein interactionDevelopment of resistancePotential for hepatotoxicity (with some inhibitors)Lack of isoform specificity (for some inhibitors)
06
Interacting drugs
Hsp90 inhibitors (small-molecule)
1 more in the full profile.
07
Biomarkers
Expression levels of Hsp90 in tumor tissueClient protein levelsSpecific downstream signaling markers
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