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FKBP prolyl isomerase 7 (FKBP7)
- Target
- FKBP7
- Molecular classification
- Enzyme, Peptidyl-prolyl cis-trans isomerase, Molecular chaperone, FKBP-type family
01
Overview
FKBP prolyl isomerase 7 (FKBP7) is an enzyme belonging to the FKBP-type peptidyl-prolyl cis/trans isomerase family. It catalyzes the cis-trans isomerization of proline residues in polypeptide chains, which accelerates protein folding during synthesis. FKBP7 functions as a molecular chaperone and is known to bind calcium. It is predominantly localized to the endoplasmic reticulum in mammalian cells and shares structural similarity to other FKBP proteins such as FKBP14. FKBP7 is characterized by its PPIase activity and FK506 drug binding capacity, but direct clinical applications or disease associations are not described in detail in the referenced literature[1][2][4][11].
- Other names
- FKBP23Peptidyl-prolyl cis-trans isomerase FKBP7PPIase FKBP7FK506-binding protein 723 kDa FK506-binding proteinFKBP-23FKBP-7RotamaseUNQ670/PRO1304PPIase
02
Mechanism of action
Immunosuppressants such as FK506 bind FKBP proteins and inhibit their PPIase activity (based on protein family data); direct mechanisms for FKBP7 specific inhibitors are not established
03
Biological functions
Protein foldingMolecular chaperone activityPeptidyl-prolyl cis/trans isomerizationCalcium ion binding
04
Disease associations
Other (no direct links to cancer, inflammation, or neurodegenerative disease established in current sources)
05
Interacting drugs
FK506/Tacrolimus (by protein family association; specific FKBP7 drug interactions not clearly described)
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