Staurosporine-induced conformational changes of cAMP-dependent protein kinase catalytic subunit explain inhibitory potential.

By L. Prade, Richard A. Engh, A. Girod, Volker Kinzel, R. Huber, D. Bossemeyer. 1997

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Interpreting linear support vector machine models with heat map molecule coloring (2011, background): “Compound C B is toxic because the red chlorobenzene substructure is not a detoxifying substructure. the binding pocket by hydrogen bonds to three protein residues: Glu121, Val123 and Thr183 [27,28].”
Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine. (2000, background): “In the Hck/quercetin complex, the analogous 3F, 4, and 5F) largely resembles the position of staurointeraction involves the 5-hydroxyl of the chromone, sporine binding to the protein kinases (Lawrie et al., while the ketone oxygen forms no apparent hydrogen 1997; Prade et al., 1997; Lamers et al., 1”