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Target intelligence / Profile preview
Heat shock protein HSP 90-alpha (HSP90AA1)
- Target
- HSP90AA1
- Molecular classification
- Molecular chaperone, Enzyme (ATPase)
01
Overview
Heat shock protein HSP 90-alpha (HSP90AA1) is a highly conserved, stress-inducible molecular chaperone. It plays a central role in maintaining cellular proteostasis, especially under conditions of proteotoxic stress. As it stabilizes many oncogenic signaling molecules, it is a validated drug target for cancer therapeutics.
- Other names
- Renal carcinoma antigen NY-REN-38Lipopolysaccharide-associated protein 2 (LAP-2)LPS-associated protein 2Heat shock protein HSP 86HSPCAHSPC1HSP86
02
Mechanism of action
Inhibition of ATP binding to the N-terminal domain, leading to disruption of chaperone function and degradation of client proteins.
03
Biological functions
Protein foldingProtein stabilizationSignal transductionApoptosis regulationCell cycle controlAntigen presentationImmune responseRegulation of protein degradation
04
Disease associations
CancerAcute upper respiratory infectionAsthma
05
Safety considerations
Potential for off-target effects due to the broad range of client proteins.Development of resistance through upregulation of alternative pathways.
06
Interacting drugs
Geldanamycin
2 more in the full profile.
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