The Crystal Structure of CHIR-AB1: A Primordial Avian Classical Fc Receptor
نویسندگان
چکیده
منابع مشابه
The crystal structure of CHIR-AB1: a primordial avian classical Fc receptor.
CHIR-AB1 is a newly identified avian immunoglobulin (Ig) receptor that includes both activating and inhibitory motifs and was therefore classified as a potentially bifunctional receptor. Recently, CHIR-AB1 was shown to bind the Fc region of chicken IgY and to induce calcium mobilization via association with the common gamma-chain, a subunit that transmits signals upon ligation of many different...
متن کاملThe chicken leukocyte receptor complex encodes a primordial, activating, high-affinity IgY Fc receptor.
Fc receptors are key players of the immune system that link the fine specificity of immunoglobulins and innate effector responses. Here, we describe a nonmammalian Fcgamma receptor, CHIR-AB1, a member of the leukocyte receptor complex, that binds IgY with high affinity with its single Ig domain. It is expressed on immature and mature B lymphocytes, monocytes, macrophages, and natural killer cel...
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We report the structure of the Fc fragment of rabbit IgG at 1.95 A (1 A=0.1 nm) resolution. Rabbit IgG was the molecule for which Porter established the four-chain, Upsilon-shaped structure of the antibody molecule, and crystals of the Fc ('Fragment crystallisable') were first reported almost 50 years ago in this journal [Porter, R. R. (1959) Biochem. J. 73, 119-126]. This high-resolution analy...
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The avian IgY antibody isotype shares a common ancestor with both mammalian IgG and IgE and so provides a means to study the evolution of their structural and functional specialisations. Although both IgG and IgE bind to their leukocyte Fc receptors with 1:1 stoichiometry, IgY binds to CHIR-AB1, a receptor expressed in avian monocytes, with 2:1 stoichiometry. The mutagenesis data reported here ...
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Herpes simplex virus type-1 expresses a heterodimeric Fc receptor, gE-gI, on the surfaces of virions and infected cells that binds the Fc region of host immunoglobulin G and is implicated in the cell-to-cell spread of virus. gE-gI binds immunoglobulin G at the basic pH of the cell surface and releases it at the acidic pH of lysosomes, consistent with a role in facilitating the degradation of an...
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ژورنال
عنوان ژورنال: Journal of Molecular Biology
سال: 2008
ISSN: 0022-2836
DOI: 10.1016/j.jmb.2008.06.082