IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v446y2007i7135d10.1038_nature05635.html
   My bibliography  Save this article

Structure of the yeast polarity protein Sro7 reveals a SNARE regulatory mechanism

Author

Listed:
  • Douglas A. Hattendorf

    (Stanford University School of Medicine, 299 Campus Drive West, Stanford, California 94305-5126, USA)

  • Anna Andreeva

    (University of North Carolina, 538 Taylor Hall, Chapel Hill, North Carolina, 27599-7090, USA)

  • Akanksha Gangar

    (University of North Carolina, 538 Taylor Hall, Chapel Hill, North Carolina, 27599-7090, USA)

  • Patrick J. Brennwald

    (University of North Carolina, 538 Taylor Hall, Chapel Hill, North Carolina, 27599-7090, USA)

  • William I. Weis

    (Stanford University School of Medicine, 299 Campus Drive West, Stanford, California 94305-5126, USA)

Abstract

The crystal structure of Sro7 and its interaction with the SNARE Sec9p is described. The structure reveals two WD40 β-propeller domains followed by a 60-residue tail. A mutant lacking the tail binds to the SNARE domain of Sec9 and inhibits assembly of the exocytic SNARE complex.

Suggested Citation

  • Douglas A. Hattendorf & Anna Andreeva & Akanksha Gangar & Patrick J. Brennwald & William I. Weis, 2007. "Structure of the yeast polarity protein Sro7 reveals a SNARE regulatory mechanism," Nature, Nature, vol. 446(7135), pages 567-571, March.
    • Handle: RePEc:nat:nature:v:446:y:2007:i:7135:d:10.1038_nature05635
    DOI: 10.1038/nature05635
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature05635
    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/nature05635?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. Marieke Meijer & Miriam Öttl & Jie Yang & Aygul Subkhangulova & Avinash Kumar & Zicheng Feng & Torben W. Voorst & Alexander J. Groffen & Jan R. T. Weering & Yongli Zhang & Matthijs Verhage, 2024. "Tomosyns attenuate SNARE assembly and synaptic depression by binding to VAMP2-containing template complexes," Nature Communications, Nature, vol. 15(1), pages 1-20, 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:446:y:2007:i:7135:d:10.1038_nature05635. 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.