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Research Article
Biomolecular Interactions of Small-molecule Inhibitors Affecting the YopH Protein Tyrosine Phosphatase
Article first published online: 13 FEB 2013
DOI: 10.1111/cbdd.12097
Published 2012. This article is a U.S. Government work and is in the public domain in the USA
Additional Information
How to Cite
Hogan, M., Bahta, M., Cherry, S., Lountos, G. T., Tropea, J. E., Zhao, B. M., Burke, T. R., Waugh, D. S. and Ulrich, R. G. (2013), Biomolecular Interactions of Small-molecule Inhibitors Affecting the YopH Protein Tyrosine Phosphatase. Chemical Biology & Drug Design, 81: 323–333. doi: 10.1111/cbdd.12097
Publication History
- Issue published online: 13 FEB 2013
- Article first published online: 13 FEB 2013
- Accepted manuscript online: 13 DEC 2012 04:31AM EST
- Received 19 October 2012, revised 3 December 2012 and accepted for publication 6 December 2012
- Abstract
- Article
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- Cited By
Keywords:
- affinity screening;
- competitive binding assay;
- high-throughput screening;
- peptide microarray;
- phosphopeptide;
- protein tyrosine phosphatase;
- surface plasmon resonance;
- Yersinia pestis outer protein H
We have developed competitive and direct binding methods to examine small-molecule inhibitors of protein tyrosine phosphatase activity. Focusing on the Yersinia pestis outer protein H, a potent bacterial protein tyrosine phosphatase, we describe how an understanding of the kinetic interactions involving Yersinia pestis outer protein H, peptide substrates, and small-molecule inhibitors of protein tyrosine phosphatase activity can be beneficial for inhibitor screening, and we further translate these results into a microarray assay for high-throughput screening.