Journal
MOLECULAR AND CELLULAR BIOCHEMISTRY
Volume 316, Issue 1-2, Pages 63-69Publisher
SPRINGER
DOI: 10.1007/s11010-008-9821-6
Keywords
protein kinase CK2; protein-protein interaction; druggable binding pocket; chemical inhibitor; podophyllotoxine indolo-analogues
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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. CK2 beta-derived cyclopeptides that target a well-defined hydrophobic pocket on CK2 alpha 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 CK2 alpha/CK2 beta interface inducing selective disruption of the CK2 alpha/CK2 beta assembly and concomitant inhibition of CK2 alpha activity.
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