IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v546y2017i7657d10.1038_nature22378.html
   My bibliography  Save this article

Human GLP-1 receptor transmembrane domain structure in complex with allosteric modulators

Author

Listed:
  • Gaojie Song

    (iHuman Institute, ShanghaiTech University)

  • Dehua Yang

    (The National Center for Drug Screening and the CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences)

  • Yuxia Wang

    (iHuman Institute, ShanghaiTech University)

  • Chris de Graaf

    (Faculty of Sciences, Amsterdam Institute for Molecules, Medicines and Systems (AIMMS), Vrije Universiteit Amsterdam)

  • Qingtong Zhou

    (iHuman Institute, ShanghaiTech University)

  • Shanshan Jiang

    (School of Pharmacy, Fudan University)

  • Kaiwen Liu

    (iHuman Institute, ShanghaiTech University
    School of Life Science and Technology, ShanghaiTech University
    University of Chinese Academy of Sciences)

  • Xiaoqing Cai

    (The National Center for Drug Screening and the CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences)

  • Antao Dai

    (The National Center for Drug Screening and the CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences)

  • Guangyao Lin

    (School of Life Science and Technology, ShanghaiTech University)

  • Dongsheng Liu

    (iHuman Institute, ShanghaiTech University)

  • Fan Wu

    (iHuman Institute, ShanghaiTech University
    School of Life Science and Technology, ShanghaiTech University
    University of Chinese Academy of Sciences)

  • Yiran Wu

    (iHuman Institute, ShanghaiTech University)

  • Suwen Zhao

    (iHuman Institute, ShanghaiTech University
    School of Life Science and Technology, ShanghaiTech University)

  • Li Ye

    (School of Pharmacy, Fudan University)

  • Gye Won Han

    (Bridge Institute, University of Southern California)

  • Jesper Lau

    (Novo Nordisk)

  • Beili Wu

    (School of Life Science and Technology, ShanghaiTech University
    University of Chinese Academy of Sciences
    The CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences)

  • Michael A. Hanson

    (GPCR Consortium, San Marcos)

  • Zhi-Jie Liu

    (iHuman Institute, ShanghaiTech University
    School of Life Science and Technology, ShanghaiTech University
    Institute of Molecular and Clinical Medicine, Kunming Medical University)

  • Ming-Wei Wang

    (The National Center for Drug Screening and the CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences
    School of Pharmacy, Fudan University
    School of Life Science and Technology, ShanghaiTech University)

  • Raymond C. Stevens

    (iHuman Institute, ShanghaiTech University
    School of Life Science and Technology, ShanghaiTech University)

Abstract

Crystal structures of the human GLP-1 receptor in complex with two negative allosteric modulators reveal a common binding pocket, and, together with mutagenesis and modelling studies, further our understanding of the receptor activation mechanism.Author: Please check the wording of the following statement, which will appear online only.

Suggested Citation

  • Gaojie Song & Dehua Yang & Yuxia Wang & Chris de Graaf & Qingtong Zhou & Shanshan Jiang & Kaiwen Liu & Xiaoqing Cai & Antao Dai & Guangyao Lin & Dongsheng Liu & Fan Wu & Yiran Wu & Suwen Zhao & Li Ye , 2017. "Human GLP-1 receptor transmembrane domain structure in complex with allosteric modulators," Nature, Nature, vol. 546(7657), pages 312-315, June.
  • Handle: RePEc:nat:nature:v:546:y:2017:i:7657:d:10.1038_nature22378
    DOI: 10.1038/nature22378
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature22378
    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/nature22378?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. Shane C. Wright & Aikaterini Motso & Stefania Koutsilieri & Christian M. Beusch & Pierre Sabatier & Alessandro Berghella & Élodie Blondel-Tepaz & Kimberley Mangenot & Ioannis Pittarokoilis & Despoina-, 2023. "GLP-1R signaling neighborhoods associate with the susceptibility to adverse drug reactions of incretin mimetics," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    2. Fenghui Zhao & Qingtong Zhou & Zhaotong Cong & Kaini Hang & Xinyu Zou & Chao Zhang & Yan Chen & Antao Dai & Anyi Liang & Qianqian Ming & Mu Wang & Li-Nan Chen & Peiyu Xu & Rulve Chang & Wenbo Feng & T, 2022. "Structural insights into multiplexed pharmacological actions of tirzepatide and peptide 20 at the GIP, GLP-1 or glucagon receptors," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    3. Janik B. Hedderich & Margherita Persechino & Katharina Becker & Franziska M. Heydenreich & Torben Gutermuth & Michel Bouvier & Moritz Bünemann & Peter Kolb, 2022. "The pocketome of G-protein-coupled receptors reveals previously untargeted allosteric sites," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    4. Xueqian Peng & Linlin Yang & Zixuan Liu & Siyi Lou & Shiliu Mei & Meiling Li & Zhong Chen & Haitao Zhang, 2022. "Structural basis for recognition of antihistamine drug by human histamine receptor," Nature Communications, Nature, vol. 13(1), pages 1-9, December.

    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:546:y:2017:i:7657:d:10.1038_nature22378. 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.