Abstract
BRAF, a serine/threonine specific protein kinase that is part of the MAPK pathway and acts as a downstream effector of RAS, is a potential therapeutic target in melanoma. We have studied a series of small-molecule BRAF inhibitors based on a 1H-imidazo[4,5-b]pyridine-2(3H)-one scaffold (ring A) as the hinge binding moiety and a number of substituted phenyl rings C that interact with the allosteric binding site. Based on molecular docking obtained by using GOLD, the interaction models on the receptor site of BRAF are guiding the design of potential inhibitory structures directed against BRAF activity.
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