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基本情報
登録情報 | データベース: PDB / ID: 1fc1 | |||||||||
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タイトル | CRYSTALLOGRAPHIC REFINEMENT AND ATOMIC MODELS OF A HUMAN FC FRAGMENT AND ITS COMPLEX WITH FRAGMENT B OF PROTEIN A FROM STAPHYLOCOCCUS AUREUS AT 2.9-AND 2.8-ANGSTROMS RESOLUTION | |||||||||
![]() | FC FRAGMENT | |||||||||
![]() | IMMUNOGLOBULIN | |||||||||
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 | ![]() | |||||||||
手法 | ![]() | |||||||||
![]() | Deisenhofer, J. | |||||||||
![]() | ![]() タイトル: Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution. 著者: Deisenhofer, J. #1: ![]() タイトル: Crystallographic Structural Studies of a Human Fc Fragment. II. A Complete Model Based on a Fourier Map at 3.5 Angstroms Resolution 著者: Deisenhofer, J. / Colman, P.M. / Epp, O. / Huber, R. #2: ![]() タイトル: Crystallographic Structural Studies of a Human Fc-Fragment. I. An Electron-Density Map at 4 Angstroms Resolution and a Partial Model 著者: Deisenhofer, J. / Colman, P.M. / Huber, R. / Haupt, H. / Schwick, G. #3: ![]() タイトル: X-Ray Studies on Antibody Fragments 著者: Colman, P.M. / Epp, O. / Fehlhammer, H. / Bode, W. / Schiffer, M. / Lattman, E.E. / Jones, T.A. | |||||||||
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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PDBx/mmCIF形式 | ![]() | 94.7 KB | 表示 | ![]() |
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PDB形式 | ![]() | 73 KB | 表示 | ![]() |
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その他 | ![]() |
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アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
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-関連構造データ
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リンク
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集合体
登録構造単位 | ![]()
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単位格子 |
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Atom site foot note | 1: THESE ATOMS WERE NOT FOUND IN THE ELECTRON DENSITY MAP. THEIR COORDINATES WERE GENERATED USING STEREOCHEMICAL CRITERIA 2: RESIDUE 374 OF EACH CHAIN IS A CIS-PROLINE. | ||||||||
詳細 | THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT CONTAINS ONE FC FRAGMENT WHICH CONSISTS OF TWO CHEMICALLY IDENTICAL POLYPEPTIDE CHAINS EACH WITH ATTACHED POLYSACCHARIDE. THESE TWO CHAINS ARE DESIGNATED CHAIN 1 AND CHAIN 2 BY THE DEPOSITOR AND REPRESENTED WITH CHAIN IDENTIFIERS A AND B BELOW. THE CH2 AND CH3 DOMAINS OF THE TWO CRYSTALLOGRAPHICALLY INDEPENDENT POLYPEPTIDE CHAINS ARE RELATED BY NON-CRYSTALLOGRAPHIC (APPROXIMATE) DIADS (SEE JRNL REFERENCE ABOVE FOR A COMPLETE DISCUSSION). THE FOLLOWING TRANSFORMATION, WHEN APPLIED TO THE CH2 DOMAIN OF CHAIN A (RESIDUES PRO A 238 THROUGH GLY A 341 TOGETHER WITH THE POLYSACCHARIDE), WILL YIELD APPROXIMATE COORDINATES FOR THE CH2 DOMAIN OF CHAIN B (RESIDUES PRO B 238 THROUGH GLY B 341 TOGETHER WITH THE POLYSACCHARIDE). TRNSF1 1 -0.99391 -0.03853 -0.10322 92.070 TRNSF2 1 -0.06679 0.95579 0.28635 -0.310 TRNSF3 1 0.08759 0.29136 -0.95207 11.160 THE FOLLOWING TRANSFORMATION, WHEN APPLIED TO THE CH3 DOMAIN OF CHAIN A (RESIDUES GLN A 342 THROUGH LEU A 443), WILL YIELD APPROXIMATE COORDINATES FOR THE CH3 DOMAIN OF CHAIN B (RESIDUES GLN B 342 THROUGH LEU B 443). TRNSF1 2 -0.99907 -0.03950 -0.01721 88.510 TRNSF2 2 -0.04232 0.97468 0.21956 -1.010 TRNSF3 2 0.00810 0.22008 -0.97544 24.570 |
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要素
#1: タンパク質 | 分子量: 25236.615 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() #2: 多糖 | Has protein modification | Y | |
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-実験情報
-実験
実験 | 手法: ![]() |
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試料調製
結晶 | マシュー密度: 2.94 Å3/Da / 溶媒含有率: 58.1 % |
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-データ収集
放射 | 散乱光タイプ: x-ray |
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放射波長 | 相対比: 1 |
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解析
精密化 | 最高解像度: 2.9 Å | ||||||||||||
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精密化ステップ | サイクル: LAST / 最高解像度: 2.9 Å
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