User:Linnea Saunders/Sandbox 1
From Proteopedia
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<StructureSection load='4f3l' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='4f3l' size='340' side='right' caption='Caption for this structure' scene=''> | ||
| - | This is a default text for your page '''Linnea Saunders/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | + | This is a default text for your page '''Linnea Saunders/Sandbox 1 '''CLOCK:BMAL1 Transcriptional Activator Complex''''''. 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. | ||
== Function == | == Function == | ||
| - | + | The circadian locomotor output cycles protein kaput and brain-muscle-arnt-like (CLOCK:BMAL1) transcriptional activator complex is an important protein involved in the regulation of our circadian rhythm. This protein interacts with DNA at regulatory elements to upregulate the production of proteins period (PER) and cryptochrome (CRY) during the day. These proteins (PER and CRY) dimerize at night and interact with CLOCK:BMAL1 to repress their own transcription. They are then degraded, allowing their transcription to occur again. This process takes approximately 24 hours and is the main mechanism of the ciracadian rhythm. CLOCK:BMAL1 lies at the heart of this process and its structure and domains are what allows it to interact with DNA and regulate the circadian rhythm. Both CLOCK and BMAL contain domains that allow them to dimerize, as well interact with DNA to regulate transcription. | |
== Disease == | == Disease == | ||
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== Structural highlights == | == Structural highlights == | ||
| - | The main domains of interest with the CLOCK:BMAL1 complex are the PAS domains which are necessary for the two proteins to dimerize, and the <scene name='84/842915/Bhlh_1/1'>basic Helix Loop Helix (bHLH) domains</scene>, which allows the complex to interact with DNA. | + | The main domains of interest with the CLOCK:BMAL1 complex are the PAS domains which are necessary for the two proteins to dimerize, and the <scene name='84/842915/Bhlh_1/1'>basic Helix Loop Helix (bHLH) domains</scene>, which allows the complex to interact with DNA. Each subunit contains two PAS domains |
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Revision as of 18:04, 24 April 2020
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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
