User:Camille Zumstein/Sandbox

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The main partners of interaction are [https://en.wikipedia.org/wiki/Calmodulin Calmodulin],
The main partners of interaction are [https://en.wikipedia.org/wiki/Calmodulin Calmodulin],
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Calcineurin is inhibited by the immunosuppressive drugs tacrolismus (FK506) or cyclosporine A (CsA). CsA and FK506 conduct their therapeutic role thought binding to the [https://en.wikipedia.org/wiki/Immunophilins immunophilins] cyclophilin and FK506 binding protein (FK506BP) respectively. The complexes CsA-cyclophilin and FK506-FK506BP bind then to calcineurin in a calcium-dependent manner thus inhibiting its phosphatase activity. Therefore the addition of these drugs to lymphocyte T prevent NFAT translocation to the nucleus and the subsequent activation its target gene.
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Calcineurin is inhibited by the immunosuppressive drugs tacrolismus (FK506) or cyclosporine A (CsA). CsA and FK506 conduct their therapeutic role thought binding to the [https://en.wikipedia.org/wiki/Immunophilins immunophilins] cyclophilin and FK506 binding protein (FK506BP) respectively. The complexes CsA-cyclophilin and FK506-FK506BP bind then to calcineurin in a calcium-dependent manner thus inhibiting its phosphatase activity. Therefore the addition of these drugs to lymphocyte T prevent NFAT translocation to the nucleus and the subsequent activation its target gene[[Ho S1, Clipstone N, Timmermann L, Northrop J, Graef I, Fiorentino D, Nourse J, Crabtree GR (1996). The mechanism of action of cyclosporin A and FK506. Clin Immunol Immunopathol. ]].

Revision as of 10:23, 7 January 2017

==Your Heading Here (maybe something like 'Structure')== 2

Caption for this structure

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References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
  3. ↑ http://www.uniprot.org/uniprot/P63329
  4. ↑ http://www.sciencedirect.com/science/article/pii/S0898656813002702
  5. ↑ http://www.rcsb.org/pdb/explore/explore.do?structureId=4IL1

Proteopedia Page Contributors and Editors (what is this?)

Camille Zumstein

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