IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v449y2007i7161d10.1038_nature06161.html
   My bibliography  Save this article

Structural basis for AMP binding to mammalian AMP-activated protein kinase

Author

Listed:
  • Bing Xiao

    (MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK)

  • Richard Heath

    (MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK
    MRC Clinical Sciences Centre, Hammersmith Hospital Campus, Imperial College, DuCane Road, London W12 0NN, UK)

  • Peter Saiu

    (MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK)

  • Fiona C. Leiper

    (MRC Clinical Sciences Centre, Hammersmith Hospital Campus, Imperial College, DuCane Road, London W12 0NN, UK)

  • Philippe Leone

    (MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK)

  • Chun Jing

    (MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK)

  • Philip A. Walker

    (MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK)

  • Lesley Haire

    (MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK)

  • John F. Eccleston

    (MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK)

  • Colin T. Davis

    (MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK)

  • Stephen R. Martin

    (MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK)

  • David Carling

    (MRC Clinical Sciences Centre, Hammersmith Hospital Campus, Imperial College, DuCane Road, London W12 0NN, UK)

  • Steven J. Gamblin

    (MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK)

Abstract

AMP-activated protein kinase (AMPK) is a central regulator of energy homeostasis in mammals. This crystal structure of the trimeric regulatory fragment of mammalian AMPK reveals the modes of AMP and ATP binding.

Suggested Citation

  • Bing Xiao & Richard Heath & Peter Saiu & Fiona C. Leiper & Philippe Leone & Chun Jing & Philip A. Walker & Lesley Haire & John F. Eccleston & Colin T. Davis & Stephen R. Martin & David Carling & Steve, 2007. "Structural basis for AMP binding to mammalian AMP-activated protein kinase," Nature, Nature, vol. 449(7161), pages 496-500, September.
  • Handle: RePEc:nat:nature:v:449:y:2007:i:7161:d:10.1038_nature06161
    DOI: 10.1038/nature06161
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature06161
    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/nature06161?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.

    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:449:y:2007:i:7161:d:10.1038_nature06161. 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.