IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v435y2005i7042d10.1038_nature03609.html
   My bibliography  Save this article

Structure of oxidized α-haemoglobin bound to AHSP reveals a protective mechanism for haem

Author

Listed:
  • Liang Feng

    (Princeton University)

  • Suiping Zhou

    (The Children's Hospital of Philadelphia and the University of Pennsylvania)

  • Lichuan Gu

    (Princeton University)

  • David A. Gell

    (University of Sydney)

  • Joel P. Mackay

    (University of Sydney)

  • Mitchell J. Weiss

    (The Children's Hospital of Philadelphia and the University of Pennsylvania)

  • Andrew J. Gow

    (The Children's Hospital of Philadelphia and the University of Pennsylvania)

  • Yigong Shi

    (Princeton University)

Abstract

Haem truths Free α-haemoglobin exists as a structurally unstable monomer and is prone to oxidation and precipitation, contributing to the pathophysiology of β-thalassaemia and other blood disorders. Molecular chaperones had long been proposed to help stabilize free α-haemoglobin, and several years ago one was discovered: α-haemoglobin stabilizing protein (AHSP), which specifically interacts with and stabilizes free α-haemoglobin. The crystal structure of AHSP bound to the oxidized Fe(III) α-haemoglobin has now been determined, revealing how the haem group is protected via a mechanism that requires α-haemoglobin to undergo drastic structural rearrangements.

Suggested Citation

  • Liang Feng & Suiping Zhou & Lichuan Gu & David A. Gell & Joel P. Mackay & Mitchell J. Weiss & Andrew J. Gow & Yigong Shi, 2005. "Structure of oxidized α-haemoglobin bound to AHSP reveals a protective mechanism for haem," Nature, Nature, vol. 435(7042), pages 697-701, June.
    • Handle: RePEc:nat:nature:v:435:y:2005:i:7042:d:10.1038_nature03609
    DOI: 10.1038/nature03609
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature03609
    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/nature03609?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:435:y:2005:i:7042:d:10.1038_nature03609. 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.