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| [[Image:1e4j.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1e4j| PDB=1e4j | SCENE= }} | | {{STRUCTURE_1e4j| PDB=1e4j | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF THE SOLUBLE HUMAN FC-GAMMA RECEPTOR III'''
| | ===CRYSTAL STRUCTURE OF THE SOLUBLE HUMAN FC-GAMMA RECEPTOR III=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_10917521}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10917521 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10917521}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Igg]] | | [[Category: Igg]] |
| [[Category: Receptor]] | | [[Category: Receptor]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:39:10 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:08:13 2008'' |
