IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v455y2008i7215d10.1038_nature07358.html
   My bibliography  Save this article

The mode of Hedgehog binding to Ihog homologues is not conserved across different phyla

Author

Listed:
  • Jason S. McLellan

    (Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA)

  • Xiaoyan Zheng

    (and)

  • Glenn Hauk

    (Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA)

  • Rodolfo Ghirlando

    (Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Disease, National Institutes of Health, Bethesda, Maryland 20892, USA)

  • Philip A. Beachy

    (and
    Howard Hughes Medical Institute Stanford University School of Medicine, Stanford, California 94305, USA)

  • Daniel J. Leahy

    (Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA)

Abstract

Hedgehog signalling: variations on the theme The Hedgehog signalling pathway specifies tissue pattern in metazoan embryos. Intriguingly, the crystal structure of the human Sonic Hedgehog protein Shh complexed with a fragment of the cell surface protein CDO (the vertebrate equivalent of Ihog in Drosophila) reveals that the mode of Hedgehog binding to Ihog homologues is not conserved across different phyla. The interaction between human Shh and CDO involves a previously unrecognized calcium-binding site in Shh that is buried at the interface between the two proteins. Mutations in Shh causing congenital malformations map to the calcium-binding site and disrupt interactions with binding partners.

Suggested Citation

  • Jason S. McLellan & Xiaoyan Zheng & Glenn Hauk & Rodolfo Ghirlando & Philip A. Beachy & Daniel J. Leahy, 2008. "The mode of Hedgehog binding to Ihog homologues is not conserved across different phyla," Nature, Nature, vol. 455(7215), pages 979-983, October.
    • Handle: RePEc:nat:nature:v:455:y:2008:i:7215:d:10.1038_nature07358
    DOI: 10.1038/nature07358
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature07358
    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/nature07358?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. Samuel C. Griffiths & Rebekka A. Schwab & Kamel El Omari & Benjamin Bishop & Ellen J. Iverson & Tomas Malinauskas & Ramin Dubey & Mingxing Qian & Douglas F. Covey & Robert J. C. Gilbert & Rajat Rohatg, 2021. "Hedgehog-Interacting Protein is a multimodal antagonist of Hedgehog signalling," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    2. Adrian On Wah Leung & Andrew Chung Hin Poon & Xue Wang & Chen Feng & Peikai Chen & Zhengfan Zheng & Michael KaiTsun To & Wilson Cheuk Wing Chan & Martin Cheung & Danny Chan, 2024. "Suppression of apoptosis impairs phalangeal joint formation in the pathogenesis of brachydactyly type A1," Nature Communications, Nature, vol. 15(1), pages 1-19, December.
    3. Wanqiu Li & Linlin Wang & Bradley M. Wierbowski & Mo Lu & Feitong Dong & Wenchen Liu & Sisi Li & Peiyi Wang & Adrian Salic & Xin Gong, 2021. "Structural insights into proteolytic activation of the human Dispatched1 transporter for Hedgehog morphogen release," Nature Communications, Nature, vol. 12(1), pages 1-11, 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:455:y:2008:i:7215:d:10.1038_nature07358. 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.