Sandbox Reserved 1656

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(New page: {{Sandbox_Reserved_ESBS20_}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> ==Your Heading Here (maybe something like 'Structure')== <StructureSection load='1stp' size='340' side='right' capti...)
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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== Function ==
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== Generalities ==
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#1 Function
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Deubiquitinase (DUB) is a key enzyme implicated in regulation of proteins degradation. Indeed, when a protein is going to be degraded, an enzymatic cascade will add a poly-ubiquitin fragment to the protein. [1] Following this step, mono or poly-ubiquitin is removed from the protein by deubiquitinase.
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#2 Families
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So far, six structural families of DUBs have been discovered. Of these, five belong to the protease family and the last is a family of zinc-dependent metallo-proteases. These enzymes do not play the same role during post-translational modifications : most families allow the removal of one of their substrates, ubiquitin, from the protein (USPs, OTUs, UCHs, Josephins, MINDYs, JAMMs, ULPs). While the Ub cascade family allows ubiquitin to be added to proteins and the UBDs family allow reading and therefore protein-ubiquitin recognition. [1]
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== Disease ==
== Disease ==
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== Relevance ==
== Relevance ==
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== References ==
== References ==
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<references/>
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[1] KOMANDER David and MEVISSEN Tycho E.T. 2017. Mechanisms of deubiquitinase specificity and regulation. Annual review of biochemistry. Vol 86,pages 159-192. DOI: https://doi.org/10.1146/annurev-biochem-061516-044916

Revision as of 11:18, 8 January 2021

This Sandbox is Reserved from 26/11/2020, through 26/11/2021 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1643 through Sandbox Reserved 1664.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

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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

[1] KOMANDER David and MEVISSEN Tycho E.T. 2017. Mechanisms of deubiquitinase specificity and regulation. Annual review of biochemistry. Vol 86,pages 159-192. DOI: https://doi.org/10.1146/annurev-biochem-061516-044916

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