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Title: Phosphorylation of cyclin-dependent kinase 2 peptides enhances metal binding.
Austin Authors: Baldwin, Graham S
Affiliation: Department of Surgery, The University of Melbourne, Austin Health, Studley Road, Heidelberg, Victoria, Australia
Issue Date: 25-Dec-2008
Publication information: Biochemical and Biophysical Research Communications 2008; 379(1): 151-4
Abstract: The cyclin-dependent kinase CDK2 is inactivated by phosphorylation on either of the two neighbouring residues Thr14 or Tyr15. The effect of phosphorylation on metal ion binding has been investigated with peptides incorporating residues 6-20 of CDK2. The stoichiometry of Ca(2+) binding increased from 1 in the un- and singly-phosphorylated peptides to 2 in the doubly phosphorylated peptide, without large changes in the affinity (75-250 microM). In contrast although binding of ferric ions to the un-phosphorylated peptide was not detected, both singly- and doubly-phosphorylated peptides bound two Fe(3+) ions. Binding of Ca(2+) or Zn(2+) ions to the doubly phosphorylated CDK2 peptide did not cause any change in absorbance, but increased the affinity of the peptide for Fe(3+) ions. These results demonstrate that double phosphorylation of CDK2 peptides increases the stoichiometry of metal ion binding, and hence may contribute to the previously observed regulation of CDK2 activity by metal ions.
Gov't Doc #: 19101503
DOI: 10.1016/j.bbrc.2008.12.027
Journal: Biochemical and biophysical research communications
Type: Journal Article
Subjects: Amino Acid Sequence
Cyclin-Dependent Kinase 2.chemistry.metabolism
Molecular Sequence Data
Protein Binding
Appears in Collections:Journal articles

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