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Biomolecular Interactions of Small‐molecule Inhibitors Affecting the YopH Protein Tyrosine Phosphatase
Author(s) -
Hogan Megan,
Bahta Medhanit,
Cherry Scott,
Lountos George T.,
Tropea Joseph E.,
Zhao Bryan M.,
Burke Terrence R.,
Waugh David S.,
Ulrich Robert G.
Publication year - 2013
Publication title -
chemical biology and drug design
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.59
H-Index - 77
eISSN - 1747-0285
pISSN - 1747-0277
DOI - 10.1111/cbdd.12097
Subject(s) - yersinia pestis , protein tyrosine phosphatase , phosphatase , small molecule , biochemistry , chemistry , tyrosine , protein–protein interaction , peptide , enzyme , biology , virulence , gene
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.

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