Cyclophilin

spinqualitylabelsall models Human Cyclophilin-A (rust, olive, turquois, dark green, khaki) complex with cyclosporin A (green, cyan, aqua, neon green, blue) (PDB entry 2x2c) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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. See also Isomerases. Cyclophilin-A has peptide cis-trans isomerase activity which regulates protein folding and trafficking . Cyclophilin-B interacts with HCV RNA polymerase and stimulates its RNA binding activity . Cyclophilin-C is a component of US2-mediated immune invasion . Cyclophilin-D is a regulator of the mitochondrial permeability transition pore . Cyclophilin-E has a role in osteoblast differentiation by increasing the transcriptional activity of Runx2 . Cyclophilin-H mediates interactions between different proteins inside the spliceosome . Cyclophilin-J has upregulated expression in human glioma . Cyclophilin-38 stabilises photosystem II in chloroplasts and supports root growth . Cyclophilin-40 modulates steroid receptor function through its association with Hsp90 . Relevance Cyp-A has a key role in immunosuppression and viral infection. Cyp-A is the target of the immunosuppressant cyclosporin A whose binding leads to the suppression of the T-cell mediated immune response. Cyp-A is required for effective HIV-1 replication in host cells. Structural highlights Cyp-A undergoes post-translational acetylation of Lys125. The acetylation modulates key functions of Cyp-A activity. 3D Structures of Cyclophilin Cyclophilin 3D structures

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