User:Linnea Saunders/Sandbox 1
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | The main domains of interest within the CLOCK:BMAL1 complex are the PAS domains which are necessary for dimerization, 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 | + | The main domains of interest within the CLOCK:BMAL1 complex are the <scene name='84/842915/Pas_domains/1'>PAS domains</scene>, which are necessary for dimerization, 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 |
== Mechanism of Interactions == | == Mechanism of Interactions == | ||
Revision as of 19:08, 26 April 2020
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References
1. 1. Li S, Wang M, Ao X, et al. CLOCK is a substrate of SUMO and sumoylation of CLOCK upregulates the transcriptional activity of estrogen receptor-α. Oncogene. 2013;32(41):4883-4891. doi:10.1038/onc.2012.518 2.Menet JS, Pescatore S, Rosbash M. CLOCK:BMAL1 is a pioneer-like transcription factor. Genes Dev. 2014;28(1):8–13. doi:10.1101/gad.228536.113
3. Takahashi JS, Hong HK, Ko CH, McDearmon EL. The genetics of mammalian circadian order and disorder: implications for physiology and disease. Nat Rev Genet. 2008;9(10):764–775. doi:10.1038/nrg2430 4. 1. Li S, Wang M, Ao X, et al. CLOCK is a substrate of SUMO and sumoylation of CLOCK upregulates the transcriptional activity of estrogen receptor-α. Oncogene. 2013;32(41):4883-4891. doi:10.1038/onc.2012.518
