Sandbox Reserved 1656
From Proteopedia
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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. | ||
- | == | + | == 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 == | ||
<references/> | <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. |
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References
- ↑ 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
- ↑ 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