IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v457y2009i7232d10.1038_nature07606.html
   My bibliography  Save this article

The Fas–FADD death domain complex structure unravels signalling by receptor clustering

Author

Listed:
  • Fiona L. Scott

    (Program in Apoptosis and Cell Death Research, The Burnham Institute for Medical Research, La Jolla, California 92037, USA
    Present address: Apoptos Inc., San Diego, California 92121, USA.)

  • Boguslaw Stec

    (Program in Apoptosis and Cell Death Research, The Burnham Institute for Medical Research, La Jolla, California 92037, USA)

  • Cristina Pop

    (Program in Apoptosis and Cell Death Research, The Burnham Institute for Medical Research, La Jolla, California 92037, USA)

  • Małgorzata K. Dobaczewska

    (Program in Apoptosis and Cell Death Research, The Burnham Institute for Medical Research, La Jolla, California 92037, USA)

  • JeongEun J. Lee

    (Program in Apoptosis and Cell Death Research, The Burnham Institute for Medical Research, La Jolla, California 92037, USA)

  • Edward Monosov

    (Program in Apoptosis and Cell Death Research, The Burnham Institute for Medical Research, La Jolla, California 92037, USA)

  • Howard Robinson

    (Brookhaven National Laboratory, Upton, New York 11973, USA)

  • Guy S. Salvesen

    (Program in Apoptosis and Cell Death Research, The Burnham Institute for Medical Research, La Jolla, California 92037, USA)

  • Robert Schwarzenbacher

    (University of Salzburg)

  • Stefan J. Riedl

    (Program in Apoptosis and Cell Death Research, The Burnham Institute for Medical Research, La Jolla, California 92037, USA)

Abstract

The complexities of cell death The crystal structure of a complex between the cell surface receptor protein Fas and the Fas-associated death domain (FADD) protein - a central feature of the so-called death-inducing signalling complex of apoptosis-inducing cellular receptors - has been determined at 2.7 Å resolution. The structure reveals a previously unknown type of death domain interaction that allows four FADD and four Fas proteins to aggregate in the one complex. Surprisingly, a conformational change opens up the Fas death domain, which creates binding surfaces for FADD as well as Fas-Fas 'bridging' interactions. Only when a sufficient number of Fas molecules are in close proximity - as is the case when Fas ligand binds - can the open form of Fas be stabilized.

Suggested Citation

  • Fiona L. Scott & Boguslaw Stec & Cristina Pop & Małgorzata K. Dobaczewska & JeongEun J. Lee & Edward Monosov & Howard Robinson & Guy S. Salvesen & Robert Schwarzenbacher & Stefan J. Riedl, 2009. "The Fas–FADD death domain complex structure unravels signalling by receptor clustering," Nature, Nature, vol. 457(7232), pages 1019-1022, February.
    • Handle: RePEc:nat:nature:v:457:y:2009:i:7232:d:10.1038_nature07606
    DOI: 10.1038/nature07606
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature07606
    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/nature07606?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. Roderick C. Slieker & Louise A. Donnelly & Elina Akalestou & Livia Lopez-Noriega & Rana Melhem & Ayşim Güneş & Frederic Abou Azar & Alexander Efanov & Eleni Georgiadou & Hermine Muniangi-Muhitu & Mahs, 2023. "Identification of biomarkers for glycaemic deterioration in type 2 diabetes," Nature Communications, Nature, vol. 14(1), pages 1-18, 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:457:y:2009:i:7232:d:10.1038_nature07606. 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.