A family of cell-membrane proteins known as G-protein-coupled receptors mediates transmembrane signal transduction. One subset of this family is the chemokine receptors, which regulate cell migration and whose activation has been implicated in a range of diseases, including immune disorders and cancer. But finding drugs that inhibit these receptors has been challenging. Two papers online in Nature^{1, 2} now describe crystal structures of two different chemokine receptors in complex with small-molecule inhibitors. Two of these antagonists bind to pockets near to the receptors' intracellular surfaces, pointing to a previously unidentified pathway that can be targeted for drug discovery.

From http://www.nature.com/nature/journal/vaop/ncurrent/full/nature20486.html

Intracellular allosteric antagonism of the CCR9 receptor. Oswald, C.et al. Nature http://dx.doi.org/10.1038/nature20606 (2016).

Structure of CC chemokine receptor 2 with orthosteric and allosteric antagonists. Zheng, Y.et al. Naturehttp://dx.doi.org/10.1038/nature20605 (2016).