Advertisement

A protein kinase switch

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

By | October 2, 2000

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.

Advertisement
Advertisement

Popular Now

  1. Most Earth-like Planet Found
  2. AAAAA Is for Arrested Translation
  3. Four-legged Snake Fossil Found
  4. The Sum of Our Parts
    Features The Sum of Our Parts

    Putting the microbiome front and center in health care, in preventive strategies, and in health-risk assessments could stem the epidemic of noncommunicable diseases.

Advertisement
Advertisement