ArticleMethods in molecular biology (Clifton, N.J.)2023
Dissecting Selectivity Determinants of Small-Molecule Inhibitors of SH2 Domains Via Fluorescence Polarization Assays.
Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Fluorescence polarization (FP) assays can be used to identify small-molecule inhibitors that bind to SH2 domain-containing proteins. We have developed FP assays by which to identify inhibitors of the SH2 domains of the two closely-related transcription factors STAT5a and STAT5b. Point mutation of selected amino acids in the putative binding site of the protein is a valuable tool by which to gain insight into the molecular mechanism of binding. In this chapter, we describe the cloning and application of point mutant proteins in order to transfer the binding preference of selected SH2 domain-binding STAT5b inhibitors to STAT5a, with results that highlight the importance of considering a role for residues outside the SH2 domain in contributing to the binding interactions of SH2 domain inhibitors.
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