Please use this identifier to cite or link to this item: http://ahro.austin.org.au/austinjspui/handle/1/10733
Title: Phosphorylation of cyclin-dependent kinase 2 peptides enhances metal binding.
Authors: Baldwin, Graham S
Affiliation: Department of Surgery, The University of Melbourne, Austin Health, Studley Road, Heidelberg, Vic, Australia. grahamsb@unimelb.edu.au
Issue Date: 25-Dec-2008
Citation: 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.
Internal ID Number: 19101503
URI: http://ahro.austin.org.au/austinjspui/handle/1/10733
DOI: 10.1016/j.bbrc.2008.12.027
URL: http://www.ncbi.nlm.nih.gov/pubmed/19101503
Type: Journal Article
Subjects: Amino Acid Sequence
Calcium.chemistry.metabolism
Cations.chemistry.metabolism
Cyclin-Dependent Kinase 2.chemistry.metabolism
Humans
Iron.chemistry.metabolism
Metals.chemistry.metabolism
Molecular Sequence Data
Peptides.chemistry.metabolism
Phosphorylation
Protein Binding
Zinc.chemistry.metabolism
Appears in Collections:Journal articles

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