Sandbox Reserved 1417
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<scene name='77/777737/Truns/1'>Scene</scene> | <scene name='77/777737/Truns/1'>Scene</scene> | ||
== Function and Mechanism == | == Function and Mechanism == | ||
| - | Ubiquitin functions as a protein that regulates the degradation of other proteins. It consists of 76 amino acids and is found in almost all cells. UBQ functions in the ubiquitin-proteasome system. In this system, ubiquitin binds to an E1 protein. This E1 protein helps transfer the ubiquitin to an E2 protein. The E2 protein then binds to an E3 protein which binds to the targeted substrate protein. After this, ubiquitin binds onto the substrate via a glysine in the <scene name='77/777737/C-terminal_glysine/1'>C-terminal</scene>. This process must occur multiple times (polyubiquitination) before the ubiquitin signals for the proteasome to bind to the substrate. The proteasome then binds to the substrate and degrades the protein. | + | Ubiquitin functions as a protein that regulates the degradation of other proteins. It consists of 76 amino acids and is found in almost all cells. UBQ functions in the ubiquitin-proteasome system. In this system, ubiquitin binds to an E1 protein. This E1 protein helps transfer the ubiquitin to an E2 protein. The E2 protein then binds to an E3 protein which binds to the targeted substrate protein. After this, ubiquitin binds onto the substrate via a glysine in the <scene name='77/777737/C-terminal_glysine/1'>C-terminal</scene>. This process must occur multiple times (polyubiquitination) before the ubiquitin signals for the proteasome to bind to the substrate. The proteasome then binds to the substrate and degrades the protein. |
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== Disease == | == Disease == | ||
Revision as of 21:03, 12 February 2018
| This Sandbox is Reserved from January through July 31, 2018 for use in the course HLSC322: Principles of Genetics and Genomics taught by Genevieve Houston-Ludlam at the University of Maryland, College Park, USA. This reservation includes Sandbox Reserved 1311 through Sandbox Reserved 1430. |
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Ubiquitin
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This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs. 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.
Function and Mechanism
Ubiquitin functions as a protein that regulates the degradation of other proteins. It consists of 76 amino acids and is found in almost all cells. UBQ functions in the ubiquitin-proteasome system. In this system, ubiquitin binds to an E1 protein. This E1 protein helps transfer the ubiquitin to an E2 protein. The E2 protein then binds to an E3 protein which binds to the targeted substrate protein. After this, ubiquitin binds onto the substrate via a glysine in the . This process must occur multiple times (polyubiquitination) before the ubiquitin signals for the proteasome to bind to the substrate. The proteasome then binds to the substrate and degrades the protein.
Disease
Relevance
Structural highlights
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
</StructureSection>
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
