Structural Characterization of Anti-Inflammatory Immunoglobulin G Fc Proteins
نویسندگان
چکیده
منابع مشابه
Structural characterization of anti-inflammatory immunoglobulin G Fc proteins.
Immunoglobulin G (IgG) is a central mediator of host defense due to its ability to recognize and eliminate pathogens. The recognition and effector responses are encoded on distinct regions of IgGs. The diversity of the antigen recognition Fab domains accounts for IgG's ability to bind with high specificity to essentially any antigen. Recent studies have indicated that the Fc effector domain als...
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Immunoglobulin G (IgG) mediates pro- and anti-inflammatory activities through the engagement of its Fc fragment (Fc) with distinct Fcg receptors (FcgRs). One class of Fc-FcgR interactions generates pro-inflammatory effects of immune complexes and cytotoxic antibodies. In contrast, therapeutic intravenous gamma globulin and its Fc fragments are anti-inflammatory. We show here that these distinct...
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A heterogeneous group of receptors binding the Fc region of Ig, Fc receptors, provides important links between the cellular and humoral branches ofthe immune system. The members of this receptor group, specific for essentially all the Ig isotypes, are expressed on a variety of cells and mediate multiple important functions. Receptors for IgG (Fc’yR) , a subgroup within the larger group of FcR, ...
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The rapidly increasing application of antibodies has inspired the development of several novel methods to isolate and target antibodies using smart biomaterials that mimic the binding of Fc-receptors to antibodies. The Fc-binding domain of antibodies is the primary binding site for e.g., effector proteins and secondary antibodies, whereas antigens bind to the Fab region. Protein A, G, and L, su...
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ژورنال
عنوان ژورنال: Journal of Molecular Biology
سال: 2014
ISSN: 0022-2836
DOI: 10.1016/j.jmb.2014.07.006