Binding domain for p21(WAF1) on the polypeptide chain of the protein kinase CK2 beta-subunit.
Protein kinase CK2 is a ubiquitous serine/threonine kinase which is involved in many proliferation-related processes in the cell. It is composed of two regulatory beta-subunits and two catalytic alpha-subunits. Its regulation still remains mysterious in spite of many years of intense research. One of its regulators is the cdk inhibitory ... molecule p21(WAF1)-a protein which is expressed in situations of genotoxic stress. p21(WAF1) binds to the beta-subunit of CK2 and inhibits the activity of CK2. Using deletion mutants of CK2 beta as well as a peptide library consisting of 15-amino-acid-long peptides derived from the polypeptide chain of CK2 beta we mapped the binding region for p21(WAF1) on the polypeptide chain of CK2 beta. We localized an amino-terminal and a carboxy-terminal binding domain. Binding of p21(WAF1) to both regions of the CK2 beta-subunit interferes with the phosphotransferase activity of the CK2 holoenzyme.
Mesh Terms:
Amino Acid Sequence, Animals, Binding Sites, Casein Kinase II, Cyclin-Dependent Kinase Inhibitor p21, Cyclins, Humans, Molecular Sequence Data, Peptide Library, Peptide Mapping, Protein Binding, Protein Structure, Quaternary, Protein Structure, Tertiary, Protein-Serine-Threonine Kinases, Recombinant Proteins, Sequence Deletion
Amino Acid Sequence, Animals, Binding Sites, Casein Kinase II, Cyclin-Dependent Kinase Inhibitor p21, Cyclins, Humans, Molecular Sequence Data, Peptide Library, Peptide Mapping, Protein Binding, Protein Structure, Quaternary, Protein Structure, Tertiary, Protein-Serine-Threonine Kinases, Recombinant Proteins, Sequence Deletion
Biochem. Biophys. Res. Commun.
Date: Feb. 24, 2000
PubMed ID: 10679299
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