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Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide

Author

Listed:
  • Arun K. Shukla

    (Duke University Medical Center)

  • Aashish Manglik

    (Molecular and Cellular Physiology, Stanford University School of Medicine)

  • Andrew C. Kruse

    (Molecular and Cellular Physiology, Stanford University School of Medicine)

  • Kunhong Xiao

    (Duke University Medical Center)

  • Rosana I. Reis

    (Duke University Medical Center)

  • Wei-Chou Tseng

    (Duke University Medical Center)

  • Dean P. Staus

    (Duke University Medical Center)

  • Daniel Hilger

    (Molecular and Cellular Physiology, Stanford University School of Medicine)

  • Serdar Uysal

    (University of Chicago)

  • Li-Yin Huang

    (Duke University Medical Center)

  • Marcin Paduch

    (University of Chicago)

  • Prachi Tripathi-Shukla

    (Duke University Medical Center)

  • Akiko Koide

    (University of Chicago)

  • Shohei Koide

    (University of Chicago)

  • William I. Weis

    (Molecular and Cellular Physiology, Stanford University School of Medicine
    Stanford University School of Medicine)

  • Anthony A. Kossiakoff

    (University of Chicago)

  • Brian K. Kobilka

    (Molecular and Cellular Physiology, Stanford University School of Medicine)

  • Robert J. Lefkowitz

    (Duke University Medical Center
    Howard Hughes Medical Institute. Duke University Medical Center
    Duke University Medical Center)

Abstract

The crystal structure of β-arrestin-1 in complex with a fully phosphorylated 29-amino-acid carboxy-terminal peptide derived from the V2 vasopressin receptor is reported; the structure of the complex shows striking conformational differences in β-arrestin-1 when compared with its inactive conformation.

Suggested Citation

  • Arun K. Shukla & Aashish Manglik & Andrew C. Kruse & Kunhong Xiao & Rosana I. Reis & Wei-Chou Tseng & Dean P. Staus & Daniel Hilger & Serdar Uysal & Li-Yin Huang & Marcin Paduch & Prachi Tripathi-Shuk, 2013. "Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide," Nature, Nature, vol. 497(7447), pages 137-141, May.
    • Handle: RePEc:nat:nature:v:497:y:2013:i:7447:d:10.1038_nature12120
    DOI: 10.1038/nature12120
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    Cited by:

    1. Hongyu Liu & Ran Duan & Xiaoyu He & Jincu Qi & Tianming Xing & Yahan Wu & Liping Zhou & Lingling Wang & Yujing Shao & Fulei Zhang & Huixing Zhou & Xingdong Gu & Bowen Lin & Yuanyuan Liu & Yan Wang & Y, 2023. "Endothelial deletion of PTBP1 disrupts ventricular chamber development," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    2. Raphael S. Haider & Edda S. F. Matthees & Julia Drube & Mona Reichel & Ulrike Zabel & Asuka Inoue & Andy Chevigné & Cornelius Krasel & Xavier Deupi & Carsten Hoffmann, 2022. "β-arrestin1 and 2 exhibit distinct phosphorylation-dependent conformations when coupling to the same GPCR in living cells," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
    3. Yasmin Aydin & Thore Böttke & Jordy Homing Lam & Stefan Ernicke & Anna Fortmann & Maik Tretbar & Barbara Zarzycka & Vsevolod V. Gurevich & Vsevolod Katritch & Irene Coin, 2023. "Structural details of a Class B GPCR-arrestin complex revealed by genetically encoded crosslinkers in living cells," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    4. Yutaro Shiraishi & Yutaka Kofuku & Takumi Ueda & Shubhi Pandey & Hemlata Dwivedi-Agnihotri & Arun K. Shukla & Ichio Shimada, 2021. "Biphasic activation of β-arrestin 1 upon interaction with a GPCR revealed by methyl-TROSY NMR," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    5. Ruibo Zhai & Zhuoqi Wang & Zhaofei Chai & Xiaogang Niu & Conggang Li & Changwen Jin & Yunfei Hu, 2023. "Distinct activation mechanisms of β-arrestin-1 revealed by 19F NMR spectroscopy," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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