Brief Communication abstract
Nature Chemical Biology 5, 394 - 396 (2009)
Published online: 26 April 2009 | doi:10.1038/nchembio.162
A new screening assay for allosteric inhibitors of cSrc
Jeffrey R Simard1, Sabine Klüter1, Christian Grütter1, Matthäus Getlik1, Matthias Rabiller1, Haridas B Rode1 & Daniel Rauh1
Targeting kinases outside the highly conserved ATP pocket is thought to be a promising strategy for overcoming bottlenecks in kinase inhibitor research, such as limited selectivity and drug resistance. Here we report the development and application of a direct binding assay to detect small molecules that stabilize the inactive conformation of the tyrosine kinase cSrc. Protein X-ray crystallography validated the assay results and confirmed an exclusively allosteric binding mode.
- Chemical Genomics Centre of the Max Planck Society, Dortmund, Germany.
Correspondence to: Daniel Rauh1 e-mail: daniel.rauh@cgc.mpg.de
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