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Conformational changes in the G protein Gs induced by the β2 adrenergic receptor

Author

Listed:
  • Ka Young Chung

    (Stanford University School of Medicine)

  • Søren G. F. Rasmussen

    (Stanford University School of Medicine
    The Panum Institute, University of Copenhagen, 2200 Copenhagen N, Denmark)

  • Tong Liu

    (Biomedical Sciences Graduate Program and UCSD DXMS Proteomics Resource, University of California San Diego)

  • Sheng Li

    (Biomedical Sciences Graduate Program and UCSD DXMS Proteomics Resource, University of California San Diego)

  • Brian T. DeVree

    (University of Michigan Medical School)

  • Pil Seok Chae

    (University of Wisconsin
    Present address: Department of Bionano Engineering, Hanyang University, Ansan 426-791, Korea.)

  • Diane Calinski

    (University of Michigan Medical School)

  • Brian K. Kobilka

    (Stanford University School of Medicine)

  • Virgil L. Woods

    (Biomedical Sciences Graduate Program and UCSD DXMS Proteomics Resource, University of California San Diego)

  • Roger K. Sunahara

    (University of Michigan Medical School)

Abstract

X-ray structure of a GPCR complex G-protein-coupled receptors (GPCRs) mediate the majority of a cell's responses to hormones and neurotransmitters, and to the senses of sight, olfaction and taste. This makes GPCRs potentially the most important group of drug targets in the human body. GPCRs are deeply embedded in the cell membrane, crossing it seven times, so structure determination for these complexes is particularly challenging — as recounted in a recent News Feature (see http://go.nature.com/ftqnx4 ). The eagerly-awaited X-ray crystal structure of a GPCR transmembrane signalling complex has now been determined by Brian Kobilka's group. The structure presented is of an agonist-occupied monomer of the β2 adrenergic receptor in complex with Gs, the stimulatory G protein for adenylyl cyclase. An accompanying paper reports the use of peptide amide hydrogen-deuterium exchange mass spectrometry to probe the protein dynamics of this signalling complex.

Suggested Citation

  • Ka Young Chung & Søren G. F. Rasmussen & Tong Liu & Sheng Li & Brian T. DeVree & Pil Seok Chae & Diane Calinski & Brian K. Kobilka & Virgil L. Woods & Roger K. Sunahara, 2011. "Conformational changes in the G protein Gs induced by the β2 adrenergic receptor," Nature, Nature, vol. 477(7366), pages 611-615, September.
    • Handle: RePEc:nat:nature:v:477:y:2011:i:7366:d:10.1038_nature10488
    DOI: 10.1038/nature10488
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    Cited by:

    1. Kevin M. Knight & Brian E. Krumm & Nicholas J. Kapolka & W. Grant Ludlam & Meng Cui & Sepehr Mani & Iya Prytkova & Elizabeth G. Obarow & Tyler J. Lefevre & Wenyuan Wei & Ning Ma & Xi-Ping Huang & Jona, 2024. "A neurodevelopmental disorder mutation locks G proteins in the transitory pre-activated state," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    2. Liang Fang & Chanjuan Zhou & Shunjie Bai & Chenglong Huang & Junxi Pan & Ling Wang & Xinfa Wang & Qiang Mao & Lu Sun & Peng Xie, 2015. "The C825T Polymorphism of the G-Protein β3 Gene as a Risk Factor for Depression: A Meta-Analysis," PLOS ONE, Public Library of Science, vol. 10(7), pages 1-11, July.
    3. Wenguang G. Liang & Juwina Wijaya & Hui Wei & Alex J. Noble & Jordan M. Mancl & Swansea Mo & David Lee & John V. Lin King & Man Pan & Chang Liu & Carla M. Koehler & Minglei Zhao & Clinton S. Potter & , 2022. "Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    4. Hongyang Li & Xin-Qiu Yao & Barry J Grant, 2018. "Comparative structural dynamic analysis of GTPases," PLOS Computational Biology, Public Library of Science, vol. 14(11), pages 1-19, November.

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