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You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Generalities
Function
Deubiquitinases or Deubiquitinating enzymes (DUBs) are key enzymes belonging to the vast group of proteases, allowing the degradation of ubiquitin of proteins. These enzymes are thus implicated in the regulation of protein degradation. Indeed, when a protein is going to be degraded, an enzymatic cascade will add a poly-ubiquitin fragment to the protein. This mechanism is called ubiquitination.[1] Following this step, mono or poly-ubiquitin is removed from the protein which has been degraded, by deubiquitinase. [3]
Families
[4]
Localization
Structure
[5]
Biological role
Disease
The involvement of deubiquitinases in diseases is still poorly understood. However, it is known that they play a role in various physiological processes, particularly in the case of cancers. [6]
Structural highlights
This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
- ↑ 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:https://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
- ↑ Amerik AY, Hochstrasser M. Mechanism and function of deubiquitinating enzymes. Biochim Biophys Acta. 2004 Nov 29;1695(1-3):189-207. doi:, 10.1016/j.bbamcr.2004.10.003. PMID:15571815 doi:https://dx.doi.org/10.1016/j.bbamcr.2004.10.003
- ↑ Amerik AY, Hochstrasser M. Mechanism and function of deubiquitinating enzymes. Biochim Biophys Acta. 2004 Nov 29;1695(1-3):189-207. doi:, 10.1016/j.bbamcr.2004.10.003. PMID:15571815 doi:https://dx.doi.org/10.1016/j.bbamcr.2004.10.003
- ↑ Johnston SC, Larsen CN, Cook WJ, Wilkinson KD, Hill CP. Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution. EMBO J. 1997 Jul 1;16(13):3787-96. PMID:9233788 doi:https://dx.doi.org/10.1093/emboj/16.13.3787
- ↑ Hamner JB. Applying the Roy adaptation model to the CCU. Crit Care Nurse. 1989 Mar;9(3):51-61. PMID:2582804