Immunophilins
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In molecular biology, immunophilins are endogenous cytosolic peptidyl-prolyl isomerases that interconvert [sic] between the cis and trans positions. They are chaperon molecules with peptidylprolyl isomerase activity that exists in two families, with different characteristics. These two families are "cyclosporin-binding cyclophilins (CyPs)" and "FK506-binding proteins (FKBPs)". However, there are also large molecules that contain both families on its opposite sides.
Immunophilins are the receptor molecules for the Immunosuppressive drugs. Immunophilins are targeted by immunosuppressive drugs such as sirolimus, cyclosporin, and tacrolimus. For these drugs in particular, known immunophilins such as cyclophilin catalyze the cis-trans isomerization of peptide bonds, particularly X-Pro peptide bonds. This prolyl isomerase activity can be inhibited by immunosuppressive drugs. Immunophilin complexes bind to calceneurin which inhibits the phosphate activity and engenders immunosuppresive effects. Immunophilins forms protein complex with ryanodine and inositol triphosphate(IP3) which impacts the release of calcium.
Cyclosoporin A(CsA), rapamaycin and FK506 act as inhibitors for immunophilin receptor proteins. The family of CsA is comprised of eleven members. However, rapamycin and FK506 are antibodies. CsA and FK506 affects the calcium dependent step of T cell response which prevents release oif interleukin-2.
See also
External links
- [1]Immunophilins at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- "Plant immunophilins and signal transduction" at berkeley.edu
- http://www.jbc.org/content/280/26/24308.full
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- ^ "Neural actions of immunophilin ligands" (PDF).
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- ^ "Neural actions of immunophilin ligands" (PDF).
