Solution Structure of the p53 Regulatory Domain of the p19ArfTumor Suppressor Protein†

Biochemistry ◽  
2001 ◽  
Vol 40 (8) ◽  
pp. 2379-2386 ◽  
Author(s):  
Enrico L. DiGiammarino ◽  
Igor Filippov ◽  
Jason D. Weber ◽  
Brian Bothner ◽  
Richard W. Kriwacki
Biochemistry ◽  
2020 ◽  
Vol 59 (44) ◽  
pp. 4238-4249
Author(s):  
Xinyue Liu ◽  
Abigail Garber ◽  
Julia Ryan ◽  
Aditi Deshpande ◽  
Dagmar Ringe ◽  
...  

2014 ◽  
Vol 426 (7) ◽  
pp. 1483-1497 ◽  
Author(s):  
Shengnan Zhang ◽  
Tao Huang ◽  
Udayar Ilangovan ◽  
Andrew P. Hinck ◽  
Paul F. Fitzpatrick

1998 ◽  
Vol 273 (25) ◽  
pp. 15633-15638 ◽  
Author(s):  
Kimmo Pääkkönen ◽  
Arto Annila ◽  
Tia Sorsa ◽  
Piero Pollesello ◽  
Carola Tilgmann ◽  
...  

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Aimee H Marceau ◽  
Caileen M Brison ◽  
Santrupti Nerli ◽  
Heather E Arsenault ◽  
Andrew C McShan ◽  
...  

Intrinsically disordered transcription factor transactivation domains (TADs) function through structural plasticity, adopting ordered conformations when bound to transcriptional co-regulators. Many transcription factors contain a negative regulatory domain (NRD) that suppresses recruitment of transcriptional machinery through autoregulation of the TAD. We report the solution structure of an autoinhibited NRD-TAD complex within FoxM1, a critical activator of mitotic gene expression. We observe that while both the FoxM1 NRD and TAD are primarily intrinsically disordered domains, they associate and adopt a structured conformation. We identify how Plk1 and Cdk kinases cooperate to phosphorylate FoxM1, which releases the TAD into a disordered conformation that then associates with the TAZ2 or KIX domains of the transcriptional co-activator CBP. Our results support a mechanism of FoxM1 regulation in which the TAD undergoes switching between disordered and different ordered structures.


2001 ◽  
Vol 268 (6) ◽  
pp. 1620-1630
Author(s):  
Yibing Wu ◽  
Yunhua Wang ◽  
Chengmin Qian ◽  
Jun Lu ◽  
Ercheng Li ◽  
...  

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