IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v556y2018i7699d10.1038_nature26153.html
   My bibliography  Save this article

Structure of the insulin receptor–insulin complex by single-particle cryo-EM analysis

Author

Listed:
  • Giovanna Scapin

    (Merck & Co.)

  • Venkata P. Dandey

    (Simons Electron Microscopy Center, National Resource for Automated Molecular Microscopy, New York Structural Biology Center)

  • Zhening Zhang

    (Simons Electron Microscopy Center, National Resource for Automated Molecular Microscopy, New York Structural Biology Center)

  • Winifred Prosise

    (Merck & Co.)

  • Alan Hruza

    (Merck & Co.)

  • Theresa Kelly

    (Merck & Co., NMR & Protein Products Characterization)

  • Todd Mayhood

    (Merck & Co., NMR & Protein Products Characterization)

  • Corey Strickland

    (Merck & Co.)

  • Clinton S. Potter

    (Simons Electron Microscopy Center, National Resource for Automated Molecular Microscopy, New York Structural Biology Center)

  • Bridget Carragher

    (Simons Electron Microscopy Center, National Resource for Automated Molecular Microscopy, New York Structural Biology Center)

Abstract

Cryo-electron microscopy structures of insulin in a complex with the insulin receptor define the S2 binding site on the receptor and suggest a mechanism for downstream propagation of insulin signalling.

Suggested Citation

  • Giovanna Scapin & Venkata P. Dandey & Zhening Zhang & Winifred Prosise & Alan Hruza & Theresa Kelly & Todd Mayhood & Corey Strickland & Clinton S. Potter & Bridget Carragher, 2018. "Structure of the insulin receptor–insulin complex by single-particle cryo-EM analysis," Nature, Nature, vol. 556(7699), pages 122-125, April.
    • Handle: RePEc:nat:nature:v:556:y:2018:i:7699:d:10.1038_nature26153
    DOI: 10.1038/nature26153
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature26153
    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/nature26153?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. Hirofumi Nagao & Ashok Kumar Jayavelu & Weikang Cai & Hui Pan & Jonathan M. Dreyfuss & Thiago M. Batista & Bruna B. Brandão & Matthias Mann & C. Ronald Kahn, 2023. "Unique ligand and kinase-independent roles of the insulin receptor in regulation of cell cycle, senescence and apoptosis," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
    2. Kohdai Yamada & Ryouhei Shioya & Kohei Nishino & Hirotake Furihata & Atsushi Hijikata & Mika K. Kaneko & Yukinari Kato & Tsuyoshi Shirai & Hidetaka Kosako & Tatsuya Sawasaki, 2023. "Proximity extracellular protein-protein interaction analysis of EGFR using AirID-conjugated fragment of antigen binding," Nature Communications, Nature, vol. 14(1), pages 1-19, December.
    3. Junhee Park & Jie Li & John P. Mayer & Kerri A. Ball & Jiayi Wu & Catherine Hall & Domenico Accili & Michael H. B. Stowell & Xiao-chen Bai & Eunhee Choi, 2022. "Activation of the insulin receptor by an insulin mimetic peptide," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    4. Robert A. Saxton & Nathanael A. Caveney & Maria Dolores Moya-Garzon & Karsten D. Householder & Grayson E. Rodriguez & Kylie A. Burdsall & Jonathan Z. Long & K. Christopher Garcia, 2023. "Structural insights into the mechanism of leptin receptor activation," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    5. Margaret Wu & Ester Carballo-Jane & Haihong Zhou & Peter Zafian & Ge Dai & Mindy Liu & Julie Lao & Terri Kelly & Dan Shao & Judith Gorski & Dmitri Pissarnitski & Ahmet Kekec & Ying Chen & Stephen F. P, 2022. "Functionally selective signaling and broad metabolic benefits by novel insulin receptor partial agonists," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    6. Nicholas S. Kirk & Qi Chen & Yingzhe Ginger Wu & Anastasia L. Asante & Haitao Hu & Juan F. Espinosa & Francisco Martínez-Olid & Mai B. Margetts & Faiz A. Mohammed & Vladislav V. Kiselyov & David G. Ba, 2022. "Activation of the human insulin receptor by non-insulin-related peptides," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    7. Junhong Kim & Na-Oh Yunn & Mangeun Park & Jihan Kim & Seongeun Park & Yoojoong Kim & Jeongeun Noh & Sung Ho Ryu & Yunje Cho, 2022. "Functional selectivity of insulin receptor revealed by aptamer-trapped receptor structures," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    8. Cristina M. Viola & Orsolya Frittmann & Huw T. Jenkins & Talha Shafi & Pierre Meyts & Andrzej M. Brzozowski, 2023. "Structural conservation of insulin/IGF signalling axis at the insulin receptors level in Drosophila and humans," Nature Communications, Nature, vol. 14(1), pages 1-13, 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:556:y:2018:i:7699:d:10.1038_nature26153. 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.