Crystal structure of the ligand-free G-protein-coupled receptor opsin

By J. Park, P. Scheerer, K. Hofmann, H. Choe, O. Ernst. Nature, 2008

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Lifting the lid on GPCRs: the role of extracellular loops (2011, background): “Active state-like structures have been obtained at low pH using the apoprotein opsin, which lacks retinal, either alone (Park et al., 2008) or complexed with a peptide corresponding to the C-terminal fragment of transducin Ga (GaCT; Scheerer et al., 2008).”
Activation mechanism of the β2-adrenergic receptor (2011, background): “Crystal structures of meta II (active) rhodopsin and of opsin (both with and without the Gα C-terminal helix bound) display a similar arrangement of helices 5, 6, and 7 (5, 21, 22), except that the intracellular end of helix 6 is shifted approximately 5 Å farther from the helical bundle in the activ”
Facilities for macromolecular crystallography at the Helmholtz-Zentrum Berlin (2012, background): “Scientists from the biophysical institute of the Charité, University Medicine Berlin, managed to gain structural insights into the ligand-free form of this GPCR, the opsin (Park et al., 2008).”