Sandbox Reserved 972

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==Structure of the complex==
==Structure of the complex==
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'''Insuline degrading enzyme (IDE)'''
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IDE (EC 3.4.24.56) is a human enzyme of the metallopeptidase family, not well-known yet. It is composed by more than 1000 residues and has a huge catalytic cavity. It is made of 2 parts linked by a loop, and it switches between an open and a close state. The size of its catalytic chamber allows the binding of peptides (70 amino acids long). IDE hydrolyzes a lot of substrates which have many differents biological activities. Its substrate can be insuline, glucagon, amyline or bradykinin.
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Bradykinin binds to the exosite.
 
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We supposed that IDE may bind two molecules of bradykinin at the same time
 
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== Function ==
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'''Bradykinin'''
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==Bradykinin==
 
Bradykinin is a short nonapeptide of the family of kinins. It's in response to an inflammatory envent and serves as a mediator of pain, inflammation and vasodilatation.
Bradykinin is a short nonapeptide of the family of kinins. It's in response to an inflammatory envent and serves as a mediator of pain, inflammation and vasodilatation.
Today, we know that kinins can be degraded by IDE.
Today, we know that kinins can be degraded by IDE.
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We supposed that IDE may bind two molecules of bradykinin at the same time
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== Function ==
==Degradation reaction of bradykinin by IDE==
==Degradation reaction of bradykinin by IDE==

Revision as of 22:50, 8 January 2015

This Sandbox is Reserved from 15/11/2014, through 15/05/2015 for use in the course "Biomolecule" taught by Bruno Kieffer at the Strasbourg University. This reservation includes Sandbox Reserved 951 through Sandbox Reserved 975.
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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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