Crystal structure of opsin in its G-protein-interacting conformation

By P. Scheerer, J. Park, Peter Werner Hildebrand, Y. Kim, N. Krauß, H. Choe, K. Hofmann, O. Ernst. Nature, 2008

1,086 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/c34f4c97b09900691c906ae54ee66e143f524f6a

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Citations in the corpus

Facilities for macromolecular crystallography at the Helmholtz-Zentrum Berlin (2012, positive): “Rhodopsin is a so-called G-protein coupled receptor or GPCR. GPCRs are seven-helix membrane proteins which are very important members of signal transduction pathways and primary targets for the pharmaceutical industry.”
Polar transmembrane interactions drive formation of ligand-specific and signal pathway-biased family B G protein-coupled receptor conformations (2013, background): “60(190), consistent with helical movements that occur in family A GPCRs (26, 34).”
GPCR Network: a large-scale collaboration on GPCR structure and function (2012, background): “Additional structure reports include the characterization of the active and inactive states for rhodopsin 36 and opsin 37 , β 2 -AR 38–41 and adenosine A 2A receptor 18,42,43 .”
Structure of a nanobody-stabilized active state of the β2 adrenoceptor (2011, methodology): “6 nM) was used as radioligand and agonist (2)-isoproterenol (ISO) or inverse agonist ICI-118,551 (ICI) as competitor.”
GPCRdb: an information system for G protein-coupled receptors (2015, background): “These have revealed mechanisms of orthosteric and allosteric (9) ligand binding, conformational changes upon receptor activation (10–12), and the modes of binding of G protein (13,14) and -arrestin (15) signal mediators.”
GPCRdb: the G protein‐coupled receptor database – an introduction (2016, background): “However, structures of fully activated receptorsaresofarlimited to complexes of β 2 -adrenoceptor to Gs (Rasmussen et al., 2011), opsin (activated rhodopsin) to β -arrestin (Kang et al., 2015), or a G t α -subunit C-terminus (Scheerer et al., 2008), and the μ”
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”