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1OW0

Crystal structure of human FcaRI bound to IgA1-Fc

Summary for 1OW0
Entry DOI10.2210/pdb1ow0/pdb
Related1OVZ
DescriptorIg alpha-1 chain C region, Immunoglobulin alpha Fc receptor, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-beta-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
Functional Keywordsiga1, fcari, cd89, antibody, fc receptor, immunoglobulin-like domain, immune system
Biological sourceHomo sapiens (human)
More
Cellular locationIsoform A. Isoform A. Isoform A. Isoform B: Secreted. Isoform B-delta-S2: Secreted: P24071
Total number of polymer chains4
Total formula weight102370.16
Authors
Herr, A.B.,Ballister, E.R.,Bjorkman, P.J. (deposition date: 2003-03-27, release date: 2003-05-27, Last modification date: 2024-11-13)
Primary citationHerr, A.B.,Ballister, E.R.,Bjorkman, P.J.
Insights into IgA-mediated immune responses from the crystal structures of human Fc-alpha-RI and its complex with IgA1-Fc
Nature, 423:614-620, 2003
Cited by
PubMed Abstract: 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.
PubMed: 12768205
DOI: 10.1038/nature01685
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

227344

數據於2024-11-13公開中

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