IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v406y2000i6793d10.1038_35018508.html
   My bibliography  Save this article

The 3.2-Å crystal structure of the human IgG1 Fc fragment–FcγRIII complex

Author

Listed:
  • Peter Sondermann

    (Max-Planck-Institut für Biochemie Abteilung Strukturforschung)

  • Robert Huber

    (Max-Planck-Institut für Biochemie Abteilung Strukturforschung)

  • Vaughan Oosthuizen

    (Max-Planck-Institut für Biochemie Abteilung Strukturforschung
    University of Port Elizabeth)

  • Uwe Jacob

    (Max-Planck-Institut für Biochemie Abteilung Strukturforschung)

Abstract

The immune response depends on the binding of opsonized antigens to cellular Fc receptors and the subsequent initiation of various cellular effector functions of the immune system. Here we describe the crystal structures of a soluble Fcγ receptor (sFcγRIII, CD16), an Fc fragment from human IgG1 (hFc1) and their complex. In the 1:1 complex the receptor binds to the two halves of the Fc fragment in contact with residues of the Cγ2 domains and the hinge region. Upon complex formation the angle between the two sFcγRIII domains increases significantly and the Fc fragment opens asymmetrically. The high degree of amino acid conservation between sFCγRIII and other Fc receptors, and similarly between hFc1 and related immunoglobulins, suggest similar structures and modes of association. Thus the described structure is a model for immune complex recognition and helps to explain the vastly differing affinities of other FcγR–IgG complexes and the FcεRIα–IgE complex.

Suggested Citation

  • Peter Sondermann & Robert Huber & Vaughan Oosthuizen & Uwe Jacob, 2000. "The 3.2-Å crystal structure of the human IgG1 Fc fragment–FcγRIII complex," Nature, Nature, vol. 406(6793), pages 267-273, July.
    • Handle: RePEc:nat:nature:v:406:y:2000:i:6793:d:10.1038_35018508
    DOI: 10.1038/35018508
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/35018508
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/35018508?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:406:y:2000:i:6793:d:10.1038_35018508. 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.