Sandbox Reserved 1644
From Proteopedia
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{{Sandbox_Reserved_ESBS20_}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_Reserved_ESBS20_}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
| - | == | + | ==2x36 - Structure of the proteolytic domain of the Human Mitochondrial Lon protease== |
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | 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 <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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| - | ==2x36 - Structure of the proteolytic domain of the Human Mitochondrial Lon protease== | ||
'''2x36''' is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. This domain belongs to the [https://en.wikipedia.org/wiki/Lon_protease_family] Lon protease family. | '''2x36''' is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. This domain belongs to the [https://en.wikipedia.org/wiki/Lon_protease_family] Lon protease family. | ||
| - | Mitochondrial Lon protease is an '''ATP-dependent serine protease''' involved in the selective degradation of abnormal proteins. [https://en.wikipedia.org/wiki/LONP1 LONP1] situated on chromosome 19 is the nuclear gene encoding mitochondrial Lon protein. The single species of [https://en.wikipedia.org/wiki/Messenger_RNA mRNA] of this protein is found in the mitochondrial matrix. This protein from human tissues has a molecular mass of 100 [https://en.wikipedia.org/wiki/Dalton_(unit) kDA]. | + | [https://en.wikipedia.org/wiki/Mitochondrion Mitochondrial] Lon [https://en.wikipedia.org/wiki/Protease protease] is an '''ATP-dependent serine protease''' involved in the selective degradation of abnormal proteins. [https://en.wikipedia.org/wiki/LONP1 LONP1] situated on chromosome 19 is the nuclear gene encoding mitochondrial Lon protein. The single species of [https://en.wikipedia.org/wiki/Messenger_RNA mRNA] of this protein is found in the mitochondrial matrix. This protein from human tissues has a molecular mass of 100 [https://en.wikipedia.org/wiki/Dalton_(unit) kDA]. |
== Function == | == Function == | ||
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| + | The mitochondrial Lon protease is an important regulator of mitochondrial [https://en.wikipedia.org/wiki/Metabolism metabolism] including the maintenance and repair of mitochondrial [https://en.wikipedia.org/wiki/DNA DNA], the homeostasis of mitochondria, and by regulating some regulatory proteins which have a short life or damaged proteins. | ||
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| + | Lon protease has three main roles. It has a [https://en.wikipedia.org/wiki/Proteolysis proteolytic] digestion of oxidized proteins | ||
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== General structure == | == General structure == | ||
Revision as of 16:14, 12 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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2x36 - Structure of the proteolytic domain of the Human Mitochondrial Lon protease
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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
