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Showing 1–7 of 7 results
Advanced filters: Author: Juan-Jose Fung Clear advanced filters

  • The X-ray crystal structure of the human β2 adrenergic receptor, a G-protein-coupled receptor, in an agonist-bound 'active' state is solved. Comparison of this structure with a previously published structure of the same GPCR in an inactive state indicates that minor changes in the binding pocket of the protein lead to major changes elsewhere — there is a large outward movement of the cytoplasmic end of one of the transmembrane segments and rearrangements of two other transmembrane segments. This structure provides insights into the process of agonist binding and activation.

    • Søren G. F. Rasmussen
    • Hee-Jung Choi
    • Brian K. Kobilka
    Research
    Nature
    Volume: 469, P: 175-180

  • The X-ray crystal structure of the human G-protein-coupled receptor protease-activated receptor 1 (PAR1) bound to the antagonist vorapaxar is solved, revealing an unusual method of drug binding that should facilitate the development of improved PAR1-selective antagonists.

    • Cheng Zhang
    • Yoga Srinivasan
    • Brian K. Kobilka
    Research
    Nature
    Volume: 492, P: 387-392

  • Here, pharmacological and biochemical evidence is provided that shows that G-protein coupling to the β2-adrenergic receptor stabilizes a ‘closed’ conformation of the G-protein-coupled receptor (GPCR) and that that the effects of the G protein on the ligand-binding site of the GPCR are observed even in the absence of a bound agonist.

    • Brian T. DeVree
    • Jacob P. Mahoney
    • Roger K. Sunahara
    Research
    Nature
    Volume: 535, P: 182-186

  • G-protein-coupled receptors (GPCRs) mediate the majority of cellular responses to hormones and neurotransmitters and are the largest group of therapeutic targets for a range of diseases. The extracellular surface (ECS) of GPCRs is diverse and therefore an ideal target for the discovery of subtype-selective drugs. Here, NMR spectroscopy is used to investigate ligand-specific conformational changes around a central structural feature in the ECS of a GPCR.

    • Michael P. Bokoch
    • Yaozhong Zou
    • Brian K. Kobilka
    Research
    Nature
    Volume: 463, P: 108-112

  • The compositional heterogeneity of proteoliposome reconstitution can skew the results of ensemble-average measurements of transmembrane protein structure and function. These compositional heterogeneities can be exploited, however, with a single-proteoliposome, high-content screening method.

    • Signe Mathiasen
    • Sune M Christensen
    • Dimitrios Stamou
    Research
    Nature Methods
    Volume: 11, P: 931-934