A small molecule–kinase interaction map for clinical kinase inhibitors View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2005-02-13

AUTHORS

Miles A Fabian, William H Biggs, Daniel K Treiber, Corey E Atteridge, Mihai D Azimioara, Michael G Benedetti, Todd A Carter, Pietro Ciceri, Philip T Edeen, Mark Floyd, Julia M Ford, Margaret Galvin, Jay L Gerlach, Robert M Grotzfeld, Sanna Herrgard, Darren E Insko, Michael A Insko, Andiliy G Lai, Jean-Michel Lélias, Shamal A Mehta, Zdravko V Milanov, Anne Marie Velasco, Lisa M Wodicka, Hitesh K Patel, Patrick P Zarrinkar, David J Lockhart

ABSTRACT

Kinase inhibitors show great promise as a new class of therapeutics. Here we describe an efficient way to determine kinase inhibitor specificity by measuring binding of small molecules to the ATP site of kinases. We have profiled 20 kinase inhibitors, including 16 that are approved drugs or in clinical development, against a panel of 119 protein kinases. We find that specificity varies widely and is not strongly correlated with chemical structure or the identity of the intended target. Many novel interactions were identified, including tight binding of the p38 inhibitor BIRB-796 to an imatinib-resistant variant of the ABL kinase, and binding of imatinib to the SRC-family kinase LCK. We also show that mutations in the epidermal growth factor receptor (EGFR) found in gefitinib-responsive patients do not affect the binding affinity of gefitinib or erlotinib. Our results represent a systematic small molecule-protein interaction map for clinical compounds across a large number of related proteins. More... »

PAGES

329-336

Journal

TITLE

Nature Biotechnology

ISSUE

3

VOLUME

23

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nbt1068

    DOI

    http://dx.doi.org/10.1038/nbt1068

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1036157274

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/15711537


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