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A protein kinase switch

William Wells

Author Affiliations

Genome Biology 2000, 1:spotlight-20000929-01  doi:10.1186/gb-spotlight-20000929-01

The electronic version of this article is the complete one and can be found online at:


Published:29 September 2000

© 2000 BioMed Central Ltd

Research news

Kinase inhibitors are plagued by a lack of specificity. Now in the 21 September Nature Bishop et al. tackle the problem by building on their earlier work, in which they modified the ATP-binding sites of Src-family tyrosine kinases to accept either nucleotide analogs or modified kinase inhibitors. In the new work the researchers mutate kinases from four distinct kinase families by replacing a bulky residue with a small residue. This change provides enough room for the binding of inhibitor analogs, which are larger than their parent inhibitors and thus do not inhibit wild-type kinases (Nature 2000, 407:395-401). The in vivo specificity is demonstrated using expression arrays. Most kinases contain a bulky residue analogous to the one mutated in this study, and thus should be amenable to the kinase-sensitization strategy.

References

  1. Exploiting chemical libraries, structure, and genomics in the search for kinase inhibitors.

    PubMed Abstract | Publisher Full Text OpenURL

  2. [http://www.nature.com/nature/] webcite

    Nature

  3. Engineering Src family protein kinases with unnatural nucleotide specificity.

    PubMed Abstract | Publisher Full Text OpenURL