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Crystal structure of opsin in its G-protein-interacting conformation
The 3.2 Å crystal structure of the bovine Ops*–GαCT peptide complex is presented and signal transfer from the receptor to the G protein nucleotide-binding site is discussed.
Crystal structure of the ligand-free G-protein-coupled receptor opsin
The crystal structure of ligand-free native opsin from bovine retinal rod cells is presented and shows prominent structural changes in the conserved E(D)RY and NPxxY(x)5,6F regions and in TM5–TM7.
Crystal structure of metarhodopsin II
By comparison with early photoproducts, it is proposed how retinal translocation and rotation induce the gross conformational changes characteristic for Meta’II, and the structures can now serve as models for the large GPCR family.
A G protein-coupled receptor at work: the rhodopsin model.
- K. Hofmann, P. Scheerer, +4 authors O. Ernst
- Biology, MedicineTrends in biochemical sciences
- 1 November 2009
G protein-coupled receptors are ubiquitous signal transducers in cell membranes, as well as important drug targets, and their activation intermediates can now be interpreted as the stepwise engagement of protein domains.
A Ligand Channel through the G Protein Coupled Receptor Opsin
The G protein coupled receptor rhodopsin contains a pocket within its seven-transmembrane helix structure, which bears the inactivating 11-cis-retinal bound by a protonated Schiff-base to Lys296 in TM7, which provides the basis for computational modeling of retinal release and uptake.
Crystal Structure of Native Opsin: the G Protein-Coupled Receptor Rhodopsin in its Ligand-free State
Structural and kinetic modeling of an activating helix switch in the rhodopsin-transducin interface
- P. Scheerer, M. Heck, +5 authors P. Hildebrand
- Chemistry, MedicineProceedings of the National Academy of Sciences
- 30 June 2009
From the 2 α5 interactions, a “helix switch” mechanism for the transition of R*·Gtαβγ·GDP to the nucleotide-free R-·G protein complex is derived that illustrates how α5 might act as a transmission rod to propagate the conformational change from the receptor-G protein interface to theucleotide binding site.
Light-induced conformational changes of the chromophore and the protein in phytochromes: bacterial phytochromes as model systems.
- P. Scheerer, N. Michael, +6 authors T. Lamparter
- Chemistry, MedicineChemphyschem : a European journal of chemical…
- 26 April 2010
Comparison of the crystal structure of an Agp1 fragment with other phytochrome crystal structures supports the idea that a light induced rearrangement of subunits within the homodimer modulates the activity of the kinase.
Opsin, a structural model for olfactory receptors?
The structure of opsin, the GPCR employed in vision, with a detergent molecule bound deep in its orthosteric ligand-binding pocket provides a template for OR homology modeling, thus enabling investigation of the structural basis of the mechanism of odorant-receptor recognition.
Differential Expression and Interaction with the Visual G-protein Transducin of Centrin Isoforms in Mammalian Photoreceptor Cells*
- A. Giessl, A. Pulvermüller, +5 authors U. Wolfrum
- Biology, MedicineJournal of Biological Chemistry
- 3 December 2004
High affinity binding to Gtβγ and subcellular localization of the centrin isoforms Cen1 and Cen2 in the connecting cilium indicated that these isoforms contribute to theCentrin-transducin complex and potentially participate in the regulation of transducin translocation through the photoreceptor cilia.