SASDDT4: Fc region of Immunoglobulin G1 (IgG1 Fc) (Immunoglobulin heavy co...

基本情報

• 登録情報: データベース: SASBDB / ID: SASDDT4

試料

Fc region of Immunoglobulin G1 (IgG1 Fc)

• Immunoglobulin heavy constant gamma 1 (protein), IgG1 Fc, Homo sapiens

機能・相同性

分子機能:

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

ドメイン・相同性:

Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold

構成要素:

Immunoglobulin heavy constant gamma 1

• 生物種: Homo sapiens (ヒト)
• 引用: ジャーナル: Structure / 年: 2018; 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 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.

登録者

• Soumya G Remesh (Lawrence Berkeley National laboratory)

モデル

• モデル #1823: ; タイプ: atomic / カイ2乗値: 0.641398787111; Omokage検索でこの集合体の類似形状データを探す (詳細)

試料

• 試料: 名称: Fc region of Immunoglobulin G1 (IgG1 Fc) / 試料濃度: 1.00-14.00
• バッファ: 名称: 20mM HEPES, 50mM NaCl / pH: 7.5

要素 #998

名称: IgG1 Fc / タイプ: protein / 記述: Immunoglobulin heavy constant gamma 1 / 分子量: 26.4 / 分子数: 2 / 由来: Homo sapiens / 参照: UniProt: P01857
配列:

TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV 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 / 線源: X-ray synchrotronシンクロトロン / 波長: 0.103 Å / スペクトロメータ・検出器間距離: 1.5 mm
• 検出器: 名称: Pilatus3 X 2M / Pixsize x: 172 mm

スキャン

タイトル: Fc region of Immunoglobulin G1 (IgG1 Fc) / 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 /

	Min	Max
Q	0.012	0.5313

距離分布関数 P(R)

ソフトウェア P(R): GNOM 5.0 / ポイント数: 753 /

	Min	Max
Q	0.01533	0.43498
P(R) point	1	753
R	0	100

結果

カーブのタイプ: merged /

	実験値	Porod
分子量	51 kDa	-
体積	-	70 nm3

	P(R)	P(R) error	Guinier	Guinier error
前方散乱 I0	420.1	0.7	414.42	1.07
慣性半径, Rg	2.7 nm	0.005	2.64 nm	0.009

	Min	Max
D	-	10
Guinier point	5	66