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- W2075427760 abstract "The conformation of a bisindolylmaleimide may be controlled by the size of a macrocyclic ring in which it is constrained. A range of techniques were used to demonstrate that the tether controls both the ratio of the two limiting conformers (syn and anti) in solution and the extent of conjugation between the maleimide and indole rings. Screening the conformationally diverse bisindolylmaleimides against a panel of protein kinases allowed their ATP binding sites to be compared using a chemical approach which, like sequence alignment, does not require detailed structural information. This approach lead to the conclusion that several AGC group protein kinases (including PKCalpha, PKCbeta, MSK1, p70 S6K, PDK-1, and MAPKAP-K1alpha) may be best inhibited by bisindolylmaleimides which adopt a compressed approximately C2-symmetric anti conformation; in constrast, GSK3beta may be best inhibited by bisindolylmaleimides whose ground state is a distorted syn conformation. It is concluded that PDK-1, whose structure has been determined by X-ray crystallography, and its mutants, may serve as particularly useful surrogates for the study of PKC inhibitors." @default.
- W2075427760 created "2016-06-24" @default.
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- W2075427760 date "2005-08-02" @default.
- W2075427760 modified "2023-09-27" @default.
- W2075427760 title "Comparison of the ATP Binding Sites of Protein Kinases Using Conformationally Diverse Bisindolylmaleimides" @default.
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- W2075427760 doi "https://doi.org/10.1021/ja050576u" @default.
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