Inhibiting receptor tyrosine kinases has been a cornerstone of cancer therapeutics for decades. Treatment strategies largely involve small-molecule kinase inhibitors and monoclonal antibodies. For receptors activated by constitutively dimeric ligands, another potential mechanism of inhibition exists: developing monomeric ligands that prevent receptor dimerization. In a recent issue of the Biochemical Journal, Zur et al. [Biochem. J. (2017) 474, 2601–2617] describe the details of creating such an inhibitor directed toward the macrophage colony-stimulating factor receptor, c-FMS. In the process of teasing apart the ligand dimer, they also uncover a potential cryptic regulatory mechanism in this receptor subfamily.
Commentary| August 31 2017
A ligand divided: antagonist, agonist and analog control
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Daryl E. Klein; A ligand divided: antagonist, agonist and analog control. Biochem J 15 September 2017; 474 (18): 3087–3088. doi: https://doi.org/10.1042/BCJ20170495
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