Structural basis for the design of bisubstrate inhibitors of protein kinase CK2 provided by complex structures with the substrate-competitive inhibitor heparin

2021 ◽  
Vol 214 ◽  
pp. 113223
Author(s):  
Alexander Schnitzler ◽  
Karsten Niefind
Keyword(s):  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Competitive Inhibitor ◽  
Structural Basis ◽  
Complex Structures ◽  
Kinase Ck2 ◽  
Bisubstrate Inhibitors

Unexpected CK2β-antagonistic functionality of bisubstrate inhibitors targeting protein kinase CK2

2020 ◽  
Vol 96 ◽  
pp. 103608 ◽  
Author(s):  
Markus Pietsch ◽  
Kaido Viht ◽  
Alexander Schnitzler ◽  
Ramesh Ekambaram ◽  
Michaela Steinkrüger ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Kinase Ck2 ◽  
Bisubstrate Inhibitors

scholarly journals The Replacement of ATP by the Competitive Inhibitor Emodin Induces Conformational Modifications in the Catalytic Site of Protein Kinase CK2

2000 ◽  
Vol 275 (38) ◽  
pp. 29618-29622 ◽  
Author(s):  
Roberto Battistutta ◽  
Stefania Sarno ◽  
Erika De Moliner ◽  
Elena Papinutto ◽  
Giuseppe Zanotti ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Competitive Inhibitor ◽  
Catalytic Site ◽  
Kinase Ck2

scholarly journals Structural basis of CX-4945 binding to human protein kinase CK2

FEBS Letters ◽  
2010 ◽  
Vol 585 (1) ◽  
pp. 104-110 ◽  
Author(s):  
Andrew D. Ferguson ◽  
Payal R. Sheth ◽  
Andrea D. Basso ◽  
Sunil Paliwal ◽  
Kimberly Gray ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Human Protein ◽  
Structural Basis ◽  
Human Protein Kinase ◽  
Kinase Ck2

scholarly journals Structural Hypervariability of the Two Human Protein Kinase CK2 Catalytic Subunit Paralogs Revealed by Complex Structures with a Flavonol- and a Thieno[2,3-d]pyrimidine-Based Inhibitor

2017 ◽  
Vol 10 (4) ◽  
pp. 9 ◽  
Author(s):  
Karsten Niefind ◽  
Nils Bischoff ◽  
Andriy Golub ◽  
Volodymyr Bdzhola ◽  
Anatoliy Balanda ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Catalytic Subunit ◽  
Human Protein ◽  
Complex Structures ◽  
Human Protein Kinase ◽  
Kinase Ck2

scholarly journals Unexpected Binding Mode of a Potent Indeno[1,2-b]indole-Type Inhibitor of Protein Kinase CK2 Revealed by Complex Structures with the Catalytic Subunit CK2α and Its Paralog CK2α′

2017 ◽  
Vol 10 (4) ◽  
pp. 98 ◽  
Author(s):  
Jennifer Hochscherf ◽  
Dirk Lindenblatt ◽  
Benedict Witulski ◽  
Robin Birus ◽  
Dagmar Aichele ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Binding Mode ◽  
Catalytic Subunit ◽  
Complex Structures ◽  
Kinase Ck2

scholarly journals 5,6-diiodo-1H-benzotriazole: new TBBt analogue that minutely affects mitochondrial activity

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Daniel Paprocki ◽  
Maria Winiewska-Szajewska ◽  
Elżbieta Speina ◽  
Róża Kucharczyk ◽  
Jarosław Poznański
Keyword(s):  
Protein Kinase ◽  
Cell Lines ◽  
Cancer Cell ◽  
Protein Kinase Ck2 ◽  
Cancer Cell Lines ◽  
Competitive Inhibitor ◽  
Attractive Alternative ◽  
Mitochondrial Activity ◽  
Mitochondrial Inner Membrane ◽  
Kinase Ck2

Abstract4,5,6,7-Tetrabromo-1H-benzotriazole is widely used as the reference ATP-competitive inhibitor of protein kinase CK2. Herein, we study its new analogs: 5,6-diiodo- and 5,6-diiodo-4,7-dibromo-1H-benzotriazole. We used biophysical (MST, ITC) and biochemical (enzymatic assay) methods to describe the interactions of halogenated benzotriazoles with the catalytic subunit of human protein kinase CK2 (hCK2α). To trace the biological activity, we measured their cytotoxicity against four reference cancer cell lines and the effect on the mitochondrial inner membrane potential. The results obtained lead to the conclusion that iodinated compounds are an attractive alternative to brominated ones. One of them retains the cytotoxicity against selected cancer cell lines of the reference TBBt with a smaller side effect on mitochondrial activity. Both iodinated compounds are candidate leaders in the further development of CK2 inhibitors.

Sign in / Sign up

Export Citation Format

Share Document