IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v540y2016i7633d10.1038_nature20606.html
   My bibliography  Save this article

Intracellular allosteric antagonism of the CCR9 receptor

Author

Listed:
  • Christine Oswald

    (Heptares Therapeutics Ltd, BioPark, Broadwater Road, Welwyn Garden City)

  • Mathieu Rappas

    (Heptares Therapeutics Ltd, BioPark, Broadwater Road, Welwyn Garden City)

  • James Kean

    (Heptares Therapeutics Ltd, BioPark, Broadwater Road, Welwyn Garden City)

  • Andrew S. Doré

    (Heptares Therapeutics Ltd, BioPark, Broadwater Road, Welwyn Garden City)

  • James C. Errey

    (Heptares Therapeutics Ltd, BioPark, Broadwater Road, Welwyn Garden City)

  • Kirstie Bennett

    (Heptares Therapeutics Ltd, BioPark, Broadwater Road, Welwyn Garden City)

  • Francesca Deflorian

    (Heptares Therapeutics Ltd, BioPark, Broadwater Road, Welwyn Garden City)

  • John A. Christopher

    (Heptares Therapeutics Ltd, BioPark, Broadwater Road, Welwyn Garden City)

  • Ali Jazayeri

    (Heptares Therapeutics Ltd, BioPark, Broadwater Road, Welwyn Garden City)

  • Jonathan S. Mason

    (Heptares Therapeutics Ltd, BioPark, Broadwater Road, Welwyn Garden City)

  • Miles Congreve

    (Heptares Therapeutics Ltd, BioPark, Broadwater Road, Welwyn Garden City)

  • Robert M. Cooke

    (Heptares Therapeutics Ltd, BioPark, Broadwater Road, Welwyn Garden City)

  • Fiona H. Marshall

    (Heptares Therapeutics Ltd, BioPark, Broadwater Road, Welwyn Garden City)

Abstract

The crystal structure of the CCR9 chemokine receptor in complex with vercirnon at 2.8 Å resolution.

Suggested Citation

  • Christine Oswald & Mathieu Rappas & James Kean & Andrew S. Doré & James C. Errey & Kirstie Bennett & Francesca Deflorian & John A. Christopher & Ali Jazayeri & Jonathan S. Mason & Miles Congreve & Rob, 2016. "Intracellular allosteric antagonism of the CCR9 receptor," Nature, Nature, vol. 540(7633), pages 462-465, December.
  • Handle: RePEc:nat:nature:v:540:y:2016:i:7633:d:10.1038_nature20606
    DOI: 10.1038/nature20606
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature20606
    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/nature20606?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. David Jonathan Wasilko & Brian S. Gerstenberger & Kathleen A. Farley & Wei Li & Jennifer Alley & Mark E. Schnute & Ray J. Unwalla & Jorge Victorino & Kimberly K. Crouse & Ru Ding & Parag V. Sahasrabud, 2024. "Structural basis for CCR6 modulation by allosteric antagonists," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    2. Xin Chen & Kexin Wang & Jianfang Chen & Chao Wu & Jun Mao & Yuanpeng Song & Yijing Liu & Zhenhua Shao & Xuemei Pu, 2024. "Integrative residue-intuitive machine learning and MD Approach to Unveil Allosteric Site and Mechanism for β2AR," Nature Communications, Nature, vol. 15(1), pages 1-17, 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. Dawei Sun & Yonglian Sun & Eric Janezic & Tricia Zhou & Matthew Johnson & Caleigh Azumaya & Sigrid Noreng & Cecilia Chiu & Akiko Seki & Teresita L. Arenzana & John M. Nicoludis & Yongchang Shi & Baome, 2023. "Structural basis of antibody inhibition and chemokine activation of the human CC chemokine receptor 8," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    5. Joshua A. Lees & João M. Dias & Francis Rajamohan & Jean-Philippe Fortin & Rebecca O’Connor & Jimmy X. Kong & Emily A. G. Hughes & Ethan L. Fisher & Jamison B. Tuttle & Gabrielle Lovett & Bethany L. K, 2023. "An inverse agonist of orphan receptor GPR61 acts by a G protein-competitive allosteric mechanism," Nature Communications, Nature, vol. 14(1), pages 1-12, 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:540:y:2016:i:7633:d:10.1038_nature20606. 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.