Cyclophilin

Source: Wikipedia, the free encyclopedia.
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
SCOP2
1cyh / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Cyclophilins (CYPs) are a family of

peptide bonds from trans form to cis form at proline residues and facilitates protein folding
.

Cyclophilin A is a

secreted
.

Mammalian cyclophilins

Human genes encoding proteins containing the cyclophilin domain include:

Cyclophilin A

Cyclophilin A + HIV peptid (green), Human.

TNF alpha and interleukin 2
.

Cyclophilin A is also known to be recruited by the Gag polyprotein during

HIV-1 virus infection, and its incorporation into new virus particles is essential for HIV-1 infectivity.[5]

Cyclophilin D

Cyclophilin D (PPIF, note that literature is confusing, the mitochondrial cyclophilin is encoded by the PPIF gene), which is located in the

mitochondria fall into a functional disorder, so the opening of the pore plays an important role in cell death
. Cyclophilin D is thought to regulate the opening of the pore because cyclosporin A, which binds to CyP-D, inhibits the pore opening.

However, mitochondria obtained from the cysts of Artemia franciscana, do not exhibit the mitochondrial permeability transition pore [8][9]

Clinical significance

Diseases

Overexpression of Cyclophilin A has been linked to poor response to inflammatory diseases, the progression or metastasis of cancer, and aging.[10]

Cyclophilins as drug targets

Cyclophilin inhibitors, such as

cyclosporin, are being developed to treat neurodegenerative diseases.[11] Cyclophilin inhibition may also be a therapy for liver diseases.[12]

References

External links