Cyclophilin
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
| - | Cyp-A undergoes post-translational acetylation of Lys125. The acetylation modulates key functions of Cyp-A activity.<ref>PMID:20364129</ref> | + | <scene name='41/415818/Cv/2'>Cyp-A undergoes post-translational acetylation of Lys125</scene>. 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 10:10, 22 December 2015
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3D Structures of Cyclophilin
Updated on 22-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
