An Unusual Binding Model of the Methyl 9-Anilinothiazolo[5,4-f] quinazoline-2-carbimidates (EHT 1610 and EHT 5372) Confers High Selectivity for Dual-Specificity …
Journal of Medicinal Chemistry, 2016•ACS Publications
Methyl 9-anilinothiazolo [5, 4-f] quinazoline-2-carbimidates 1 (EHT 5372) and 2 (EHT 1610)
are strong inhibitors of DYRK's family kinases. The crystal structures of the complex revealed
a noncanonical binding mode of compounds 1 and 2 in DYRK2, explaining the remarkable
selectivity and potency of these inhibitors. The structural data and comparison presented
here provide therefore a template for further improvement of this inhibitor class and for the
development of novel inhibitors selectively targeting DYRK kinases.
are strong inhibitors of DYRK's family kinases. The crystal structures of the complex revealed
a noncanonical binding mode of compounds 1 and 2 in DYRK2, explaining the remarkable
selectivity and potency of these inhibitors. The structural data and comparison presented
here provide therefore a template for further improvement of this inhibitor class and for the
development of novel inhibitors selectively targeting DYRK kinases.
Methyl 9-anilinothiazolo[5,4-f]quinazoline-2-carbimidates 1 (EHT 5372) and 2 (EHT 1610) are strong inhibitors of DYRK’s family kinases. The crystal structures of the complex revealed a noncanonical binding mode of compounds 1 and 2 in DYRK2, explaining the remarkable selectivity and potency of these inhibitors. The structural data and comparison presented here provide therefore a template for further improvement of this inhibitor class and for the development of novel inhibitors selectively targeting DYRK kinases.
ACS Publications