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Cyclophilin
From Proteopedia
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== Function == | == Function == | ||
| - | [[Cyclophilin]] (Cyp) binds cyclosporin. They are peptidylprolyl isomerases which catalyze the isomerisation of proline. The '''Cyp-A/cyclosporin A''' complex inhibits organ rejection. '''Cyp-D''' is a component of the mitochondria permeability pore. Rotamase such as FKBP is a prokaryotic Cyp which is not inhibited by cyclosporin but by FK-506 – an immunosuppressive drug. <ref>PMID:14731520</ref> | + | [[Cyclophilin]] (Cyp) binds cyclosporin. They are peptidylprolyl isomerases which catalyze the isomerisation of proline. The '''Cyp-A/cyclosporin A''' complex inhibits organ rejection. '''Cyp-D''' is a component of the mitochondria permeability pore. Rotamase such as FKBP is a prokaryotic Cyp which is not inhibited by cyclosporin but by FK-506 – an immunosuppressive drug. <ref>PMID:14731520</ref> See also [[Isomerases]]. |
== Relevance == | == Relevance == | ||
Revision as of 11:46, 10 February 2016
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3D Structures of Cyclophilin
Updated on 10-February-2016
References
- ↑ Stamnes MA, Rutherford SL, Zuker CS. Cyclophilins: a new family of proteins involved in intracellular folding. Trends Cell Biol. 1992 Sep;2(9):272-6. PMID:14731520
- ↑ Lammers M, Neumann H, Chin JW, James LC. Acetylation regulates cyclophilin A catalysis, immunosuppression and HIV isomerization. Nat Chem Biol. 2010 May;6(5):331-7. Epub 2010 Apr 4. PMID:20364129 doi:10.1038/nchembio.342
