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Double trouble

Nature Structural Biology volume 8, pages 16–18 (2001)Cite this article

An efficient bisubstrate inhibitor of insulin receptor tyrosine kinase has been created by connecting modules that target the ATP- and peptide-binding sites.

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Figure 1: The domain organization of representative tyrosine kinases.
Figure 2: Schematic diagram showing how a bivalent protein kinase inhibitor simultaneously engages the ATP and peptide binding sites of a kinase catalytic domain.
Figure 3: Three-dimensional structure of the bivalent tyrosine kinase inhibitor bound to the IRK catalytic domain5.

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  1. the Department of Physiology and Biophysics, State University of New York at Stony Brook, Stony Brook, 11794-8661, New York, USA

    W. Todd Miller

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  1. W. Todd Miller
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Miller, W. Double trouble. Nat Struct Mol Biol 8, 16–18 (2001). https://doi.org/10.1038/82986

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