Cyclophilin
From Proteopedia
(Difference between revisions)
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| - | <StructureSection load='2x2c' size='350' side='right' caption='Human Cyclophilin-A with cyclosporin A (PDB entry [[2x2c]])' scene=''> | + | <StructureSection load='2x2c' size='350' side='right' caption='Human Cyclophilin-A (rust, olive, turquois,dark green, khaki) complex with cyclosporin A (green, cyan, aqua, neon green, blue) (PDB entry [[2x2c]])' scene=''> |
== Function == | == Function == | ||
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== Relevance == | == 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. | |
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| + | == Structural highlights == | ||
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| + | Cyp-A undergoes post-translational acetylation of Lys125. The acetylation modulates key functions of Cyp-A activity.<ref>PMID:20364129</ref> | ||
</StructureSection> | </StructureSection> | ||
== 3D Structures of Cyclophilin == | == 3D Structures of Cyclophilin == | ||
Revision as of 08:54, 17 December 2015
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3D Structures of Cyclophilin
Updated on 17-December-2015
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
