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Identification of chemical inhibitors of protein-kinase CK2 subunit interaction.

Abstract : Protein kinase CK2 is a multi-subunit complex whose dynamic assembly appears as a crucial point of regulation. The ability to interfere with specific protein-protein interactions has already provided powerful means of influencing the functions of selected proteins within the cell. CK2beta-derived cyclopeptides that target a well-defined hydrophobic pocket on CK2alpha have been previously characterized as potent inhibitors of CK2 subunit assembly [9]. As a first step toward the rational design of low molecular weight CK2 antagonists, we have in the present study screened a collection of podophyllotoxine indolo-analogues to identify chemical inhibitors of the CK2 subunit interaction. We report the identification of a podophyllotoxine indolo-analogue as a chemical ligand that binds to the CK2alpha/CK2beta interface inducing selective disruption of the CK2alpha/CK2beta assembly and concomitant inhibition of CK2alpha activity.
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https://www.hal.inserm.fr/inserm-00413239
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Submitted on : Thursday, September 3, 2009 - 3:37:47 PM
Last modification on : Monday, January 3, 2022 - 3:12:30 PM

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Béatrice Laudet, Virginie Moucadel, Renaud Prudent, Odile Filhol, yung-Sing Wong, et al.. Identification of chemical inhibitors of protein-kinase CK2 subunit interaction.. Molecular and Cellular Biochemistry, Springer Verlag, 2008, 316 (1-2), pp.63-9. ⟨10.1007/s11010-008-9821-6⟩. ⟨inserm-00413239⟩

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