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データを開く
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基本情報
登録情報 | データベース: SASBDB / ID: SASDDV4 |
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![]() | Fc-region of Immunoglobulin G1, M135Y/S137T/T139E mutant (IgG1 Fc-YTE)
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機能・相同性 | ![]() Fc-gamma receptor I complex binding / complement-dependent cytotoxicity / IgG immunoglobulin complex / antibody-dependent cellular cytotoxicity / immunoglobulin receptor binding / immunoglobulin complex, circulating / Classical antibody-mediated complement activation / Initial triggering of complement / FCGR activation / complement activation, classical pathway ...Fc-gamma receptor I complex binding / complement-dependent cytotoxicity / IgG immunoglobulin complex / antibody-dependent cellular cytotoxicity / immunoglobulin receptor binding / immunoglobulin complex, circulating / Classical antibody-mediated complement activation / Initial triggering of complement / FCGR activation / complement activation, classical pathway / Role of phospholipids in phagocytosis / antigen binding / FCGR3A-mediated IL10 synthesis / Regulation of Complement cascade / B cell receptor signaling pathway / FCGR3A-mediated phagocytosis / Regulation of actin dynamics for phagocytic cup formation / antibacterial humoral response / Interleukin-4 and Interleukin-13 signaling / blood microparticle / adaptive immune response / extracellular space / extracellular exosome / extracellular region / plasma membrane 類似検索 - 分子機能 |
生物種 | ![]() |
![]() | ![]() タイトル: Conformational Plasticity of the Immunoglobulin Fc Domain in Solution. 著者: Soumya G Remesh / Anthony A Armstrong / Andrew D Mahan / Jinquan Luo / Michal Hammel / ![]() 要旨: Fragment crystallizable (Fc) region of immunoglobulin G (IgG) antibody binds to specific Fc receptors (FcγRs) to control antibody effector functions. Currently, engineered specific Fc-FcγR ...Fragment crystallizable (Fc) region of immunoglobulin G (IgG) antibody binds to specific Fc receptors (FcγRs) to control antibody effector functions. Currently, engineered specific Fc-FcγR interactions are validated with a static conformation derived from the crystal structure. However, computational evidence suggests that the conformational variability of Fcs plays an important role in receptor recognition. Here we elucidate Fc flexibility of IgG1, IgG2, and IgG1 Fc with mutations (M255Y/S257T/T259E) in solution by small-angle X-ray scattering (SAXS). Measured SAXS profiles and experimental parameters show variations in flexibility between Fc isotypes. We develop and apply a modeling tool for an accurate conformational sampling of Fcs followed by SAXS fitting. Revealed conformational variability of the CH2 domain as low as 10 Å in displacement, illustrates the power of the atomistic modeling combined with SAXS. This inexpensive SAXS-based approach offers to improve the engineering of antibodies for tailoring Fc receptor interactions through altering and measuring Fc flexibility. |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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ダウンロードとリンク
-モデル
モデル #1825 | ![]() タイプ: atomic / カイ2乗値: 0.70651480336 ![]() |
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試料
![]() | 名称: Fc-region of Immunoglobulin G1, M135Y/S137T/T139E mutant (IgG1 Fc-YTE) 試料濃度: 1.00-14.00 |
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バッファ | 名称: 20 mM HEPES, 50mM NaCl / pH: 7.5 |
要素 #997 | 名称: IgG1 Fc-YTE / タイプ: protein 記述: Immunoglobulin heavy constant gamma 1 M255Y/S257T/T259E 分子量: 26.6 / 分子数: 2 / 由来: Homo sapiens / 参照: UniProt: P01857 配列: TCPPCPAPEL LGGPSVFLFP PKPKDTLYIT REPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT ...配列: TCPPCPAPEL LGGPSVFLFP PKPKDTLYIT REPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK |
-実験情報
ビーム | 設備名称: Advanced Light Source (ALS) 12.3.1 (SIBYLS) / 地域: Berkeley, CA / 国: USA ![]() | ||||||||||||||||||||||||||||||||||||
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検出器 | 名称: Pilatus3 X 2M / Pixsize x: 172 mm | ||||||||||||||||||||||||||||||||||||
スキャン | 測定日: 2016年2月17日 / 保管温度: 4 °C / セル温度: 20 °C / 照射時間: 0.3 sec. / フレーム数: 33 / 単位: 1/A /
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