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  1. The molecular mechanisms and the cellular function of GPCR-βarr interactions were particularly well studied using the arginine-vasopressin (AVP) V2 receptor (V2R), which is involved in the control of water reabsorption and urine concentration in the kidney (10, 11).This archetypal model system is well suited to analyze GPCR-βarr assembly because of a long-lasting and stable interaction.
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      microscopy active structure of the wild-type arginine-vasopressin V2 receptor (V2R) in complex with -arrestin1. It reveals an atypical position of -arrestin1 compared to previously described GPCR-arrestin assemblies, associated with an original V2R/ -arrestin1 interface involving all receptor intracellular loops. Phosphorylated sites of the

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  3. pubmed.ncbi.nlm.nih.gov

    Here, we report the cryo-electron microscopy active structure of the wild-type arginine-vasopressin V2 receptor (V2R) in complex with β-arrestin1. It reveals an atypical position of β-arrestin1 compared to previously described GPCR-arrestin assemblies, associated with an original V2R/β-arrestin1 interface involving all receptor intracellular ...
  4. ncbi.nlm.nih.gov

    National Center for Biotechnology Information

    https://www.ncbi.nlm.nih.gov › pmc › articles › PMC10866553

    The structure of the vasopressin-V2 receptor-β-arrestin1 complex provides original insights into GPCR-arrestin architecture. INTRODUCTION The biological role of arrestins in G protein-coupled receptor (GPCR) regulation was first found in the visual system more than 40 years ago, when arrestin1 was shown to bind to the light-activated ...
    Publication:Sci Adv. 2022 Sep; 8(35): eabo7761.
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  6. researchgate.net

    (C) Final 3D model of the complex. from publication: Structure of the vasopressin hormone-V2 receptor-β-arrestin1 ternary complex | Arrestins interact with G protein-coupled receptors ...
  7. Here, we report the cryo-electron microscopy active structure of the wild-type arginine-vasopressin V2 receptor (V2R) in complex with β-arrestin1. It reveals an atypical position of β-arrestin1 compared to previously described GPCR-arrestin assemblies, associated with an original V2R/β-arrestin1 interface involving all receptor intracellular ...
  8. semanticscholar.org

    Cryo-electron microscopy active structure of the wild-type arginine-vasopressin V2 receptor (V2R) in complex with β-arrestin1 reveals an atypical position of β-Arrestin 1 compared to previously described GPCR-argentin assemblies, associated with an original V2R/β-arRestin1 interface involving all receptor intracellular loops. Arrestins interact with G protein-coupled receptors (GPCRs) to ...
  9. sciencedirect.com

    Jan 1, 2023The retosiban-bound human OTR 3D structure is the first AVP/OT receptor structure released and the only one determined using X-ray crystallography (Waltenspühl, Schöppe, Ehrenmann, Kummer, & Plückthun, 2020). ... Structure of the vasopressin hormone-V2 receptor-β-arrestin1 ternary complex. Science Advances (2022) J. Bous et al. Cryo ...
  10. pubmed.ncbi.nlm.nih.gov

    The information from structure determination was herein exploited to build a structural model of the ternary complex, comprising fully phosphorylated V2 vasopressin receptor (V2R), the agonist arginine vasopressin (AVP), and β-arrestin 1 (β-arr1). Molecular simulations served to explore dynamics and structural communication in the ternary ...
  11. researchgate.net

    Structure of the vasopressin hormone-V2 receptor- -arrestin1 ternary complex Julien Bous 1,2 †‡, Aurélien Fouillen 1,2 †, Hélène Orcel 2 , Stefano Trapani 1 , Xiaojing Cong 2 ,
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