IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v505y2014i7482d10.1038_nature12815.html
   My bibliography  Save this article

Structural basis of lentiviral subversion of a cellular protein degradation pathway

Author

Listed:
  • David Schwefel

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

  • Harriet C. T. Groom

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

  • Virginie C. Boucherit

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

  • Evangelos Christodoulou

    (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)

  • Jonathan P. Stoye

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

  • Kate N. Bishop

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

  • Ian A. Taylor

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

Abstract

The crystal structure of a ternary complex of the lentiviral accessory protein Vpx with the E3 ligase substrate adaptor DCAF1 and the HIV-1 restriction factor SAMHD1 shows how Vpx recruits SAMHD1 to the cell’s ubiquitination machinery.

Suggested Citation

  • David Schwefel & Harriet C. T. Groom & Virginie C. Boucherit & Evangelos Christodoulou & Philip A. Walker & Jonathan P. Stoye & Kate N. Bishop & Ian A. Taylor, 2014. "Structural basis of lentiviral subversion of a cellular protein degradation pathway," Nature, Nature, vol. 505(7482), pages 234-238, January.
  • Handle: RePEc:nat:nature:v:505:y:2014:i:7482:d:10.1038_nature12815
    DOI: 10.1038/nature12815
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature12815
    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/nature12815?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. Oliver J. Acton & Devon Sheppard & Simone Kunzelmann & Sarah J. Caswell & Andrea Nans & Ailidh J. O. Burgess & Geoff Kelly & Elizabeth R. Morris & Peter B. Rosenthal & Ian A. Taylor, 2024. "Platform-directed allostery and quaternary structure dynamics of SAMHD1 catalysis," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    2. Jung-Eun Park & Tae-Sung Kim & Yan Zeng & Melissa Mikolaj & Jong Ahn & Muhammad S. Alam & Christina M. Monnie & Victoria Shi & Ming Zhou & Tae-Wook Chun & Frank Maldarelli & Kedar Narayan & Jinwoo Ahn, 2024. "Centrosome amplification and aneuploidy driven by the HIV-1-induced Vpr•VprBP•Plk4 complex in CD4+ T cells," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    3. Martin Schröder & Martin Renatus & Xiaoyou Liang & Fabian Meili & Thomas Zoller & Sandrine Ferrand & Francois Gauter & Xiaoyan Li & Frederic Sigoillot & Scott Gleim & Therese-Marie Stachyra & Jason R., 2024. "DCAF1-based PROTACs with activity against clinically validated targets overcoming intrinsic- and acquired-degrader resistance," Nature Communications, Nature, vol. 15(1), pages 1-19, 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:505:y:2014:i:7482:d:10.1038_nature12815. 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.