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Identification of Allosteric Inhibitors of p21-Activated Kinase

  • Julien Viaud
  • Jeffrey R. PetersonEmail author
Protocol
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Part of the Methods in Molecular Biology book series (MIMB, volume 928)

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.

Key words

Kinase inhibitor Protein kinase Pak kinase Autoinhibition Allosteric inhibition Cdc42 Rho GTPases GTP-binding protein 

Notes

Acknowledgments

This work described here was supported by a W.W. Smith Foundation Award and an American Cancer Society Scholar Award to J.R.P. and by a National Institutes of Health (NIH) award RO1 GM083025 to J.R.P.

J.V. was supported by a grant from the Fondation pour la Recherche Médicale.

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Copyright information

© Springer Science+Business Media New York 2012

Authors and Affiliations

  1. 1.Cancer Biology ProgramFox Chase Cancer CenterPhiladelphiaUSA

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