IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v457y2009i7226d10.1038_nature07614.html
   My bibliography  Save this article

Structural basis for androgen specificity and oestrogen synthesis in human aromatase

Author

Listed:
  • Debashis Ghosh

    (Structural Biology, Hauptman-Woodward Medical Research Institute, 700 Ellicott Street, Buffalo, New York 14203, USA
    Pharmacology and Therapeutics, Roswell Park Cancer Institute, Elm and Carlton Streets, Buffalo, New York 14263, USA)

  • Jennifer Griswold

    (Structural Biology, Hauptman-Woodward Medical Research Institute, 700 Ellicott Street, Buffalo, New York 14203, USA)

  • Mary Erman

    (Structural Biology, Hauptman-Woodward Medical Research Institute, 700 Ellicott Street, Buffalo, New York 14203, USA)

  • Walter Pangborn

    (Structural Biology, Hauptman-Woodward Medical Research Institute, 700 Ellicott Street, Buffalo, New York 14203, USA)

Abstract

Human placental aromatase structure Aromatase cytochrome P450 is the only enzyme in vertebrates known to catalyse the biosynthesis of all oestrogens from androgens. This enzyme catalyses the three-step conversion of androstenedione, testosterone, and 16α-hydroxytestosterone to oestrone, 17β-oestradiol, and 17β,16α-oestriol (respectively). Inhibitors of aromatase are potential therapeutics for oestrogen-dependent breast cancer. In this paper, Ghosh et al. solve the X-ray crystal structure of the first natural mammalian, full-length P450, human placental aromatase. The locations of catalytically important residues shed new light on the reaction mechanism of this enzyme, and it may be possible to utilize this information to develop new aromatase inhibitors.

Suggested Citation

  • Debashis Ghosh & Jennifer Griswold & Mary Erman & Walter Pangborn, 2009. "Structural basis for androgen specificity and oestrogen synthesis in human aromatase," Nature, Nature, vol. 457(7226), pages 219-223, January.
    • Handle: RePEc:nat:nature:v:457:y:2009:i:7226:d:10.1038_nature07614
    DOI: 10.1038/nature07614
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature07614
    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/nature07614?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:457:y:2009:i:7226:d:10.1038_nature07614. 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.