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== Structural highlights ==
== Structural highlights ==
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PDE5 is a dimeric protein of about 270 amino acids long. C terminal has the catalytic domain and N temrinal has the regulatory domain, the GAF domain. The GAF domain "mediates the allosteric regulation of the bond with cGMP" ( à reforuler :http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2518390/)
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PDE5 is a dimeric protein of about 270 amino acids long. The C terminal has the catalytic domain and two Zn2+ binding site and N temrinal is the regulatory domain which includes two the GAF domain a and b. There are thus plural allosteric binding site for cGMP in the Cterminal and the N terminal. cGAMP binds on Gap a allosteric site and promotes the phosphorylation of SER 92 of PKG. This phosphorylation increases the affinity betwezen cGMP and PDE5 : another cGMP binds to the Gapb which allows the activation of the catalytic site of PDE5. :http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2518390/)

Revision as of 08:01, 27 January 2016

This Sandbox is Reserved from 15/12/2015, through 15/06/2016 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1120 through Sandbox Reserved 1159.
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Human PDE5 structure and its inhibitor 5R

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
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