Journal article

Phosphorylation of cyclin-dependent kinase 2 peptides enhances metal binding

Graham S Baldwin

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | ACADEMIC PRESS INC ELSEVIER SCIENCE | Published : 2009

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 caus..

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University of Melbourne Researchers

Grants

Awarded by National Health and Medical Research Council of Australia


Awarded by National Institutes of Health


Awarded by NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES


Funding Acknowledgements

We thank Dr. H.-C. Cheng (University of Melbourne) for generous gifts of the CDK2 and pY-CDK2 peptides and Drs. H.-C. Cheng, A. Ferrand and R.S. Norton for many helpful discussions. This work was Supported in part by grants from the National Health and Medical Research Council of Australia (400062, 454322) and the National Institutes of Health (5RO1GM065926-05).