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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2000-07

AUTHORS

Peter Sondermann, Robert Huber, Vaughan Oosthuizen, Uwe Jacob

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 Fc gamma receptor (sFc gammaRIII, 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 C gamma2 domains and the hinge region. Upon complex formation the angle between the two sFc gammaRIII domains increases significantly and the Fc fragment opens asymmetrically. The high degree of amino acid conservation between sFc gammaRIII 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 Fc gammaR-IgG complexes and the Fc epsilonRI alpha-IgE complex. More... »

PAGES

267

Journal

TITLE

Nature

ISSUE

6793

VOLUME

406

Author Affiliations

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/35018508

    DOI

    http://dx.doi.org/10.1038/35018508

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1024812761

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/10917521


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