IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v477y2011i7366d10.1038_nature10488.html
   My bibliography  Save this article

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
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature10488
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature10488?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. 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.
    2. 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.
    3. 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.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:477:y:2011:i:7366:d:10.1038_nature10488. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.