Protein-coding gene in humans
FKBP5 |
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![](https://upload.wikimedia.org/wikipedia/commons/thumb/1/15/Protein_FKBP5_PDB_1kt0.png/250px-Protein_FKBP5_PDB_1kt0.png) |
Available structures |
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PDB | Ortholog search: PDBe RCSB |
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List of PDB id codes |
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1KT0, 3O5D, 3O5E, 3O5F, 3O5G, 3O5I, 3O5J, 3O5K, 3O5L, 3O5M, 3O5O, 3O5P, 3O5Q, 3O5R, 4DRH, 4DRI, 4DRK, 4DRM, 4DRN, 4DRO, 4DRP, 4DRQ, 4JFI, 4JFJ, 4JFK, 4JFL, 4JFM, 4R0X, 4TW6, 4TW7, 4TX0, 4W9O, 4W9P, 4W9Q, 5DIT, 5DIU, 5BXJ, 5DIV |
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Identifiers |
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Aliases | FKBP5, AIG6, FKBP51, FKBP54, P54, PPIase, Ptg-10, FK506 binding protein 5, FKBP prolyl isomerase 5 |
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External IDs | OMIM: 602623 MGI: 104670 HomoloGene: 3038 GeneCards: FKBP5 |
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Wikidata |
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FK506 binding protein 5, also known as FKBP5, is a protein which in humans is encoded by the FKBP5 gene.[5]
Function
The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds to the immunosuppressants tacrolimus (FK506) and sirolimus (rapamycin). It is thought to mediate calcineurin inhibition. It also interacts functionally with mature corticoid receptor hetero-complexes (i.e. progesterone-, glucocorticoid-, mineralocorticoid-receptor complexes) along with the 90 kDa heat shock protein and PTGES3 (P23 protein).[6]
As an Hsp90-associated co-chaperone that regulates the responsiveness of steroid hormone receptors, FKBP51 plays an important role in stress endocrinology and glucocorticoid signaling.[6]
Clinical significance
The FKBP5 gene has been found to have multiple polyadenylation sites[5] and is statistically associated with a higher rate of depressive disorders.[7]
Decreased methylation in the promoter of the FKBP5 gene has been observed in blood samples from patients with neurodegenerative diseases.[8]
FKBP51 Ligands
As a key player in several diseases like stress-related disorders, chronic pain, and obesity, FKBP51 is an attractive drug target. SAFit2 currently the most best characterized FKBP51 ligand, has shown promising effects in numerous animal models.[6] Macrocyclic FKBP51-selective ligands are non-immunosuppressive, engage FKBP51 in cells, and block the cellular effect of FKBP51.[9]