Abstract
Protein kinases are among the most important drug targets; however the structural conservation of the ATP-binding pocket of kinases can lead to promiscuous inhibition of additional unintended kinase targets. Allosteric inhibitors that target less conserved regions of protein kinases represent an alternative approach that may provide more selective kinase inhibition. In this report, protocols are provided for the screening and identification of Pak1 inhibitors acting via an allosteric mechanism.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Allosteric Regulation
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Animals
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Drug Design
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GTP-Binding Proteins / metabolism
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Protein Kinase Inhibitors / chemistry*
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Protein Kinase Inhibitors / pharmacology*
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Protein Serine-Threonine Kinases / metabolism
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Sf9 Cells
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p21-Activated Kinases / antagonists & inhibitors*
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p21-Activated Kinases / metabolism
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rho GTP-Binding Proteins
Substances
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Protein Kinase Inhibitors
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Protein Serine-Threonine Kinases
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p21-Activated Kinases
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GTP-Binding Proteins
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rho GTP-Binding Proteins