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-基本情報
登録情報 | データベース: SASBDB / ID: SASDDH2 |
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試料 | Aglycosylated Human Immunoglobulin G Fc Region
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機能・相同性 | 機能・相同性情報 補体依存性細胞傷害 / 抗体依存性細胞傷害 / Fc-gamma receptor I complex binding / Classical antibody-mediated complement activation / IgG immunoglobulin complex / Initial triggering of complement / FCGR activation / Role of phospholipids in phagocytosis / immunoglobulin complex, circulating / immunoglobulin receptor binding ...補体依存性細胞傷害 / 抗体依存性細胞傷害 / Fc-gamma receptor I complex binding / Classical antibody-mediated complement activation / IgG immunoglobulin complex / Initial triggering of complement / FCGR activation / Role of phospholipids in phagocytosis / immunoglobulin complex, circulating / immunoglobulin receptor binding / complement activation, classical pathway / FCGR3A-mediated IL10 synthesis / antigen binding / Regulation of Complement cascade / FCGR3A-mediated phagocytosis / B cell receptor signaling pathway / Regulation of actin dynamics for phagocytic cup formation / antibacterial humoral response / Interleukin-4 and Interleukin-13 signaling / 獲得免疫系 / blood microparticle / extracellular space / extracellular exosome / extracellular region / 細胞膜 類似検索 - 分子機能 |
生物種 | Homo sapiens (ヒト) |
引用 | ジャーナル: MAbs / 年: 2019 タイトル: C2 domain orientation of human immunoglobulin G in solution: Structural comparison of glycosylated and aglycosylated Fc regions using small-angle X-ray scattering. 著者: Seiki Yageta / Hiroshi Imamura / Risa Shibuya / Shinya Honda / 要旨: The N-linked glycan in immunoglobulin G is critical for the stability and function of the crystallizable fragment (Fc) region. Alteration of these protein properties upon the removal of the N-linked ...The N-linked glycan in immunoglobulin G is critical for the stability and function of the crystallizable fragment (Fc) region. Alteration of these protein properties upon the removal of the N-linked glycan has often been explained by the alteration of the C2 domain orientation in the Fc region. To confirm this hypothesis, we examined the small-angle X-ray scattering (SAXS) profile of the glycosylated Fc region (gFc) and aglycosylated Fc region (aFc) in solution. Conformational characteristics of the C2 domain orientation were validated by comparison with SAXS profiles theoretically calculated from multiple crystal structures of the Fc region with different C2 domain orientations. The reduced chi-square values from the fitting analyses of gFc and aFc associated with the degree of openness or closure of each crystal structure, as determined from the first principal component that partially governed the variation of the C2 domain orientation extracted by a singular value decomposition analysis. For both gFc and aFc, the best-fitted SAXS profiles corresponded to ones calculated based on the crystal structure of gFc that formed a "semi-closed" C2 domain orientation. Collectively, the data indicated that the removal of the N-linked glycan only negligibly affected the C2 domain orientation in solution. These findings will guide the development of methodology for the production of highly refined functional Fc variants. |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-モデル
モデル #2722 | タイプ: atomic / カイ2乗値: 0.026 / P-value: 0.010176 Omokage検索でこの集合体の類似形状データを探す (詳細) |
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-試料
試料 | 名称: Aglycosylated Human Immunoglobulin G Fc Region / 試料濃度: 3.19 mg/ml |
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バッファ | 名称: 20 mM Citrate-Phosphate / pH: 7 |
要素 #935 | 名称: aFc / タイプ: protein / 記述: Aglycosylated human immunoglobulin G Fc region / 分子量: 25.651 / 分子数: 2 / 由来: Homo sapiens / 参照: UniProt: P01857 配列: ADKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSREEMT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN ...配列: ADKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSREEMT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGK |
-実験情報
ビーム | 設備名称: Photon Factory (PF), High Energy Accelerator Research Organization (KEK) BL-10C 地域: Tsukuba / 国: Japan / 線源: X-ray synchrotronシンクロトロン / 波長: 0.12 Å / スペクトロメータ・検出器間距離: 2 mm | |||||||||||||||||||||||||||||||||
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検出器 | 名称: Pilatus3 2M / Pixsize x: 0.172 mm | |||||||||||||||||||||||||||||||||
スキャン | タイトル: Aglycosylated Human Immunoglobulin G Region / 測定日: 2017年3月5日 / セル温度: 25 °C / 照射時間: 2 sec. / フレーム数: 15 / 単位: 1/A /
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距離分布関数 P(R) | ソフトウェア P(R): GNOM 5.0 / ポイント数: 351 /
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結果 | カーブのタイプ: single_conc
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