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Biochemical, cellular and structural characterization of novel and selective ERK3 inhibitors.
Grädler, Ulrich; Busch, Michael; Leuthner, Birgitta; Raba, Michael; Burgdorf, Lars; Lehmann, Martin; Linde, Nina; Esdar, Christina.
Afiliación
  • Grädler U; Merck KGaA, Frankfurter Str. 250, D-64293 Darmstadt, Germany. Electronic address: ulrich.graedler@merckgroup.com.
  • Busch M; Merck KGaA, Frankfurter Str. 250, D-64293 Darmstadt, Germany.
  • Leuthner B; Merck KGaA, Frankfurter Str. 250, D-64293 Darmstadt, Germany.
  • Raba M; Crelux GmbH - a WuXi AppTec Company, Am Klopferspitz 19 a, D-82152 München, Germany.
  • Burgdorf L; Merck KGaA, Frankfurter Str. 250, D-64293 Darmstadt, Germany.
  • Lehmann M; Merck KGaA, Frankfurter Str. 250, D-64293 Darmstadt, Germany.
  • Linde N; Merck KGaA, Frankfurter Str. 250, D-64293 Darmstadt, Germany.
  • Esdar C; Merck KGaA, Frankfurter Str. 250, D-64293 Darmstadt, Germany.
Bioorg Med Chem Lett ; 30(22): 127551, 2020 11 15.
Article en En | MEDLINE | ID: mdl-32927028
Triazolo[4,5-d]pyrimidin-5-amines were identified from kinase selectivity screening as novel ERK3 inhibitors with sub-100 nanomolar potencies in a biochemical assay using MK5 as substrate and with an attractive kinase selectivity profile. ERK3 crystal structures clarified the inhibitor binding mode in the ATP pocket with impact on A-loop, GC-loop and αC-helix conformations suggesting a potential structural link towards MK5 interaction via the FHIEDE motif. The inhibitors also showed sub-100 nM potencies in a cellular ERK3 NanoBRET assay and with excellent correlation to the biochemical IC50s. This novel series provides valuable tool compounds to further investigate the biological function and activation mechanism of ERK3.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteína Quinasa 6 Activada por Mitógenos / Inhibidores de Proteínas Quinasas Límite: Humans Idioma: En Revista: Bioorg Med Chem Lett Asunto de la revista: BIOQUIMICA / QUIMICA Año: 2020 Tipo del documento: Article Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteína Quinasa 6 Activada por Mitógenos / Inhibidores de Proteínas Quinasas Límite: Humans Idioma: En Revista: Bioorg Med Chem Lett Asunto de la revista: BIOQUIMICA / QUIMICA Año: 2020 Tipo del documento: Article Pais de publicación: Reino Unido