FKBP14 Human
Description
Product Specs
Product Science Overview
FKBP14 is a 22-kilodalton protein that contains several important structural motifs:
- Peptidyl-prolyl isomerase domain: This domain is responsible for the protein’s enzymatic activity, specifically catalyzing the cis-trans isomerization of proline residues in polypeptide chains. This activity is crucial for proper protein folding and function.
- EF-hand motifs: These are helix-loop-helix structural domains capable of binding calcium ions, which play a role in various cellular processes.
- Endoplasmic reticulum (ER) retention signal: This signal ensures that FKBP14 is retained within the ER, where it performs its functions related to protein folding and quality control .
FKBP14 is primarily located in the endoplasmic reticulum and is involved in the folding and assembly of newly synthesized proteins. It acts as a chaperone, assisting in the proper folding of proteins that contain proline residues. This function is essential for maintaining cellular homeostasis and preventing the accumulation of misfolded proteins, which can lead to various diseases.
Mutations in the FKBP14 gene have been associated with a rare genetic disorder known as FKBP14-related Ehlers-Danlos syndrome (EDS). This condition is characterized by joint hypermobility, skin hyperextensibility, and other connective tissue abnormalities. The discovery of FKBP14’s role in this syndrome has provided valuable insights into the molecular mechanisms underlying connective tissue disorders .
FKBP14, like other members of the FKBP family, has been the subject of extensive research due to its involvement in various cellular processes and its potential as a therapeutic target. The ability of FKBP14 to bind immunosuppressive drugs such as FK506 and rapamycin has made it a valuable tool in studying immune regulation and developing new treatments for autoimmune diseases and transplant rejection .
