SASDDU4: Fc region of Immunoglobulin G2 (IgG2 Fc) (Immunoglobulin heavy co...

基本情報

• 登録情報: データベース: SASBDB / ID: SASDDU4

試料

Fc region of Immunoglobulin G2 (IgG2 Fc)

• Immunoglobulin heavy constant gamma 2 (protein), IgG2 Fc S257A, Homo sapiens

機能・相同性

分子機能:

IgG immunoglobulin complex / 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 / blood microparticle / adaptive immune response / extracellular space / extracellular exosome / extracellular region / plasma membrane

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 2

• 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 #1824: ; タイプ: atomic / カイ2乗値: 2.99812598286; 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 G2 (IgG2 Fc) / 試料濃度: 1.00-12.00
• バッファ: 名称: 20mM HEPES, 50mM NaCl / pH: 7.5

要素 #999

名称: IgG2 Fc S257A / タイプ: protein / 記述: Immunoglobulin heavy constant gamma 2 / 分子量: 26.2 / 分子数: 2 / 由来: Homo sapiens / 参照: UniProt: P01859
配列:

VECPPCPAPP VAGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVQ FNWYVDGVEV HNAKTKPREE QFNSTFRVVS VLTVVHQDWL NGKEYKCKVS NKGLPAPIEK TISKTKGQPR EPQVYTLPPS REEMTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPMLDSDGSF 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 / 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 G2 (IgG2 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	0.0148	0.5397

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	0.01812	0.43777
P(R) point	1	753
R	0	90

結果

カーブのタイプ: merged /

	実験値	Porod
分子量	51 kDa	-
体積	-	67 nm3

	P(R)	P(R) error	Guinier	Guinier error
前方散乱 I0	1.043	0.003	1.058	0.001
慣性半径, Rg	2.7 nm	0.003	2.77 nm	0.005

	Min	Max	Error
D	-	9	0.01
Guinier point	3	60	-