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Showing 1–19 of 19 results
Advanced filters: Author: Xavier Deupi Clear advanced filters

  • Lengthy molecular dynamics simulations of complex systems at the atomic scale usually require supercomputers. Now, by stitching together many shorter independent simulations run 'in the cloud', this requirement has been circumvented, allowing two milliseconds of the dynamics of a G-protein-coupled receptor to be simulated.

    • Xavier Deupi
    News & Views
    Nature Chemistry
    Volume: 6, P: 7-8

  • Extensive mutant cycle analysis provides a map of the residues that contribute to stability and activation-associated conformational dynamics of the Gαi1 protein in nucleotide-bound states and in complex with the G protein–coupled receptor rhodopsin.

    • Dawei Sun
    • Tilman Flock
    • Dmitry B Veprintsev
    Research
    Nature Structural & Molecular Biology
    Volume: 22, P: 686-694

  • Rhodospsin is a G-protein-coupled receptor that is responsible for vision in dim light. Light isomerizes the protein's retinal chromophore and triggers concerted movements of several transmembrane helices. Here, an approach involving mutant rhodopsins and infrared spectroscopy enabled changes in the electrostatic environment to be seen as rhodopsin proceeded along its activation pathway. Early conformational changes were observed that precede the well-known larger movements of the transmembrane helices.

    • Shixin Ye
    • Ekaterina Zaitseva
    • Reiner Vogel
    Research
    Nature
    Volume: 464, P: 1386-1389

  • Opsins are responsible for light perception across the animal kingdom. Here the authors show cryo-EM structures of an activated bistable opsin, shedding light on the activation mechanism of this class of bidirectional photoswitches.

    • Oliver Tejero
    • Filip Pamula
    • Ching-Ju Tsai
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-13

  • One picosecond after photoactivation, isomerized retinal pulls away from half of its numerous interactions with its binding pocket, and the excess of the photon energy is released through an anisotropic protein breathing motion in the direction of the extracellular space.

    • Thomas Gruhl
    • Tobias Weinert
    • Valerie Panneels
    ResearchOpen Access
    Nature
    Volume: 615, P: 939-944

  • Here the authors present improved intramolecular sensors for β-arrestin2 and 1, which enable assessment of conformational changes of both isoforms in living cells. These reveal that the same GPCR induces differential conformational rearrangements that determine the functional diversity between the two β-arrestins.

    • Raphael S. Haider
    • Edda S. F. Matthees
    • Carsten Hoffmann
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-17

  • The cellular functions of arrestins are determined in part by the pattern of phosphorylation on the G protein-coupled receptors (GPCRs) to which arrestins bind. Here, authors use a library of synthetic phosphopeptide analogues of the GPCR rhodopsin C-terminus and determine the ability of these peptides to bind and activate arrestins using a variety of biochemical and biophysical methods.

    • Daniel Mayer
    • Fred F. Damberger
    • Dmitry B. Veprintsev
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-14

  • GPCRmd is a community-driven online platform to visualize, analyze and share G-protein-coupled receptor (GPCR) molecular dynamics data. It currently contains simulation data representing 100% of GPCR classes, 71% of receptor subtypes and 80% of GPCR families.

    • Ismael Rodríguez-Espigares
    • Mariona Torrens-Fontanals
    • Jana Selent
    Research
    Nature Methods
    Volume: 17, P: 777-787

  • Although several X-ray crystal structures of G protein-coupled receptors (GPCRs) have been reported, relatively little is known about the conformational dynamics of these important membrane proteins; here, the authors used NMR spectroscopy to monitor the conformational changes that occur in the turkey β1-adrenergic receptor in the presence of antagonists, partial agonists, and full agonists.

    • Shin Isogai
    • Xavier Deupi
    • Stephan Grzesiek
    Research
    Nature
    Volume: 530, P: 237-241

  • A systematic investigation of high-resolution G-protein-coupled receptor (GPCR) structures uncovers a conserved inter-helical network of non-covalent contacts that defines the GPCR fold, and provides insights into the molecular determinants of different GPCR conformations.

    • A. J. Venkatakrishnan
    • Xavier Deupi
    • M. Madan Babu
    Reviews
    Nature
    Volume: 494, P: 185-194

  • An interactive online resource integrated in the GPCRdb hub presents tools to design GPCR constructs and determine appropriate experimental conditions for structural studies by crystallography and cryo-EM.

    • Christian Munk
    • Eshita Mutt
    • David E. Gloriam
    Reviews
    Nature Methods
    Volume: 16, P: 151-162

  • Takashi Nagata et al. use UV-visible spectroscopic analysis to show that Ser186 increases the retinylidene Schiff base (SB) pKa of a spider rhodopsin in the inactive state but not after light activation. The change in contribution of Ser186 to the SB pKa suggests that the counterion (Glu181)–SB interaction rearranges upon light activation.

    • Takashi Nagata
    • Mitsumasa Koyanagi
    • Akihisa Terakita
    ResearchOpen Access
    Communications Biology
    Volume: 2, P: 1-9