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Target intelligence / Profile preview
Chaperonin 10 (cpn10)
- Target
- cpn10
- Molecular classification
- Molecular chaperone, Chaperonin
01
Overview
Chaperonin 10 (cpn10), also known as Hsp10 or GroES, is a molecular chaperone essential for proper protein folding. It functions as a co-chaperone with cpn60 (Hsp60/GroEL), forming a crucial chaperonin system in prokaryotes, mitochondria, and chloroplasts. Cpn10 forms a heptameric ring that binds to cpn60, creating an isolated environment for protein folding in an ATP-dependent manner. It plays a role in folding newly synthesized or stress-denatured proteins, preventing aggregation, supporting mitochondrial function, and participating in processes like apoptosis, inflammation, and carcinogenesis through its involvement in protein homeostasis.
- Other names
- Heat shock protein 10Hsp10GroES (in Escherichia coli)Early-pregnancy factor (EPF, in humans)
02
Biological functions
Protein foldingPrevention of protein aggregationMitochondrial functionProtein homeostasis
03
Disease associations
ApoptosisInflammationCarcinogenesis
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