Elucidation of a cell receptor's crystal structure has revealed a unique lateral docking mechanism, report Hugh Rosen of the Scripps Research Institute in La Jolla, California, and his colleagues.
G-protein-coupled receptors (GPCRs) are signalling molecules that span the plasma membranes of cells and are generally activated by external molecules that pass through a channel-like opening into a binding site. However, the researchers determined the crystal structure of the sphingosine 1-phosphate receptor 1 (S1P1, pictured) and showed that the receptor is triggered by certain lipids passing through the plasma membrane and binding through the lateral docking mechanism. They also found that S1P1 has atypical binding sites in less conserved regions of the docking site and that compounds that adhere to these activate S1P1 more specifically than do lipids.
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Sideways activation. Nature 482, 442 (2012). https://doi.org/10.1038/482442c
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DOI: https://doi.org/10.1038/482442c
