Target intelligence / Profile preview

Heat shock protein HSP90-alpha (HSP90AA1)

Target
HSP90AA1
Molecular classification
Molecular chaperone, Enzyme
01

Overview

Heat shock protein HSP90-alpha (HSP90AA1) is a highly conserved and essential molecular chaperone involved in the folding, stabilization, and regulation of a wide array of client proteins, many of which are critical for cell signaling, growth, and survival. It functions as an ATP-dependent chaperone, assisting in protein folding, refolding, and stabilization. HSP90-alpha plays a central role in cancer due to its stabilization of multiple oncogenic signaling molecules, making it a therapeutic target for anti-cancer agents.

Other names
HSPCAHSPC1HSP90AHSP86 ProteinHeat shock 86 kDa protein alpha (cytosolic), member A1Renal carcinoma antigen NY-REN-38Lipopolysaccharide-associated protein 2 (LAP-2)LPS-associated protein 2
02

Mechanism of action

Inhibition of ATPase activity, leading to destabilization and degradation of client proteins.

03

Biological functions

Protein foldingProtein stabilizationRegulation of client proteinsSignal transductionCell growthCell survival
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.
06

Interacting drugs

Geldanamycin derivatives (e.g., BIIB021)

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