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Issue 5, 2013
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CDC25A-inhibitory RE derivatives bind to pocket adjacent to the catalytic site

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Abstract

RE derivatives, which are cell-permeable and non-electrophilic dual-specificity protein phosphatase inhibitors developed in our laboratory, inhibit CDC25A/B non-competitively, as determined by means of kinetic experiments. To identify the binding site of RE derivatives, we designed and synthesized the new probe molecule RE142, having a Michael acceptor functionality for covalent bond formation with the enzyme, a biotin tag to enable enrichment of probe-bound peptide(s), and a chemically cleavable linker to facilitate release of probe-bound peptides from avidin beads. LC-MS analysis indicated that RE142 binds to one of the residues Cys384-Tyr386 of CDC25A, within a pocket adjacent to the catalytic site.

Graphical abstract: CDC25A-inhibitory RE derivatives bind to pocket adjacent to the catalytic site

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Publication details

The article was received on 01 Jan 2013, accepted on 10 Feb 2013 and first published on 11 Feb 2013


Article type: Paper
DOI: 10.1039/C3MB00003F
Citation: Mol. BioSyst., 2013,9, 1026-1034
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    CDC25A-inhibitory RE derivatives bind to pocket adjacent to the catalytic site

    A. Tsuchiya, M. Asanuma, G. Hirai, K. Oonuma, M. Muddassar, E. Nishizawa, Y. Koyama, Y. Otani, K. Y. J. Zhang and M. Sodeoka, Mol. BioSyst., 2013, 9, 1026
    DOI: 10.1039/C3MB00003F

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