The reversible phosphorylation process is a key driver in the regulation of protein function. Protein kinases, one of the largest gene families, are an integral part of this phenomenon. These enzymes are involved in numerous cellular mechanisms including cell cycle, signal transduction, gene expression and apoptosis. As such, protein kinases have been targeted in drug discovery spanning multiple therapeutic areas, among them, oncology, diabetes and inflammation. A major challenge facing this research is identifying small molecule inhibitors, which bind potently to the kinase of interest, while remaining selective versus other members of the family. Fortunately, the availability of X-ray structures has assisted in this endeavor, by elucidating structural and conformational features of protein kinases that might be targeted for enhanced potency and specificity. Some of these strategies will be presented herein.
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