1ovz

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==Overview==
==Overview==
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Immunoglobulin-alpha (IgA)-bound antigens induce immune effector responses, by activating the IgA-specific receptor FcalphaRI (CD89) on immune cells., Here we present crystal structures of human FcalphaRI alone and in a, complex with the Fc region of IgA1 (Fcalpha). FcalphaRI has two, immunoglobulin-like domains that are oriented at approximately right, angles to each other. Fcalpha resembles the Fcs of immunoglobulins IgG and, IgE, but has differently located interchain disulphide bonds and external, rather than interdomain N-linked carbohydrates. Unlike 1:1 FcgammaRIII:IgG, and Fc epsilon RI:IgE complexes, two FcalphaRI molecules bind each Fcalpha, dimer, one at each Calpha2-Calpha3 junction. The FcalphaRI-binding site on, IgA1 overlaps the reported polymeric immunoglobulin receptor, (pIgR)-binding site, which might explain why secretory IgA cannot initiate, phagocytosis or bind to FcalphaRI-expressing cells in the absence of an, integrin co-receptor.
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Immunoglobulin-alpha (IgA)-bound antigens induce immune effector responses by activating the IgA-specific receptor FcalphaRI (CD89) on immune cells. Here we present crystal structures of human FcalphaRI alone and in a complex with the Fc region of IgA1 (Fcalpha). FcalphaRI has two immunoglobulin-like domains that are oriented at approximately right angles to each other. Fcalpha resembles the Fcs of immunoglobulins IgG and IgE, but has differently located interchain disulphide bonds and external rather than interdomain N-linked carbohydrates. Unlike 1:1 FcgammaRIII:IgG and Fc epsilon RI:IgE complexes, two FcalphaRI molecules bind each Fcalpha dimer, one at each Calpha2-Calpha3 junction. The FcalphaRI-binding site on IgA1 overlaps the reported polymeric immunoglobulin receptor (pIgR)-binding site, which might explain why secretory IgA cannot initiate phagocytosis or bind to FcalphaRI-expressing cells in the absence of an integrin co-receptor.
==About this Structure==
==About this Structure==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Ballister, E.R.]]
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[[Category: Ballister, E R.]]
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[[Category: Bjorkman, P.J.]]
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[[Category: Bjorkman, P J.]]
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[[Category: Herr, A.B.]]
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[[Category: Herr, A B.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: TRS]]
[[Category: TRS]]
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[[Category: immunoglobulin-like domain]]
[[Category: immunoglobulin-like domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:36:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:22:14 2008''

Revision as of 12:22, 21 February 2008


1ovz, resolution 3.00Å

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Crystal structure of human FcaRI

Overview

Immunoglobulin-alpha (IgA)-bound antigens induce immune effector responses by activating the IgA-specific receptor FcalphaRI (CD89) on immune cells. Here we present crystal structures of human FcalphaRI alone and in a complex with the Fc region of IgA1 (Fcalpha). FcalphaRI has two immunoglobulin-like domains that are oriented at approximately right angles to each other. Fcalpha resembles the Fcs of immunoglobulins IgG and IgE, but has differently located interchain disulphide bonds and external rather than interdomain N-linked carbohydrates. Unlike 1:1 FcgammaRIII:IgG and Fc epsilon RI:IgE complexes, two FcalphaRI molecules bind each Fcalpha dimer, one at each Calpha2-Calpha3 junction. The FcalphaRI-binding site on IgA1 overlaps the reported polymeric immunoglobulin receptor (pIgR)-binding site, which might explain why secretory IgA cannot initiate phagocytosis or bind to FcalphaRI-expressing cells in the absence of an integrin co-receptor.

About this Structure

1OVZ is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Insights into IgA-mediated immune responses from the crystal structures of human FcalphaRI and its complex with IgA1-Fc., Herr AB, Ballister ER, Bjorkman PJ, Nature. 2003 Jun 5;423(6940):614-20. Epub 2003 May 21. PMID:12768205

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