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Biomolecular Interactions of small-molecule inhibitors affecting the YopH protein tyrosine phosphatase.

ABSTRACT: 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.

SUBMITTER: Hogan M

PROVIDER: S-EPMC3573263 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature

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Biomolecular Interactions of small-molecule inhibitors affecting the YopH protein tyrosine phosphatase.

Hogan Megan M Bahta Medhanit M Cherry Scott S Lountos George T GT Tropea Joseph E JE Zhao Bryan M BM Burke Terrence R TR Waugh David S DS Ulrich Robert G RG

Chemical biology & drug design 20130301 3

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 the ...[more]

PMID: 23241354

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