1OW0
Crystal structure of human FcaRI bound to IgA1-Fc
1OW0 の概要
エントリーDOI | 10.2210/pdb1ow0/pdb |
関連するPDBエントリー | 1OVZ |
分子名称 | Ig 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) |
機能のキーワード | iga1, fcari, cd89, antibody, fc receptor, immunoglobulin-like domain, immune system |
由来する生物種 | Homo sapiens (human) 詳細 |
細胞内の位置 | Isoform A. Isoform A. Isoform A. Isoform B: Secreted. Isoform B-delta-S2: Secreted: P24071 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 102370.16 |
構造登録者 | |
主引用文献 | Herr, 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: 12768205DOI: 10.1038/nature01685 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.1 Å) |
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