1C3D
X-RAY CRYSTAL STRUCTURE OF C3D: A C3 FRAGMENT AND LIGAND FOR COMPLEMENT RECEPTOR 2
1C3D の概要
| エントリーDOI | 10.2210/pdb1c3d/pdb |
| 分子名称 | C3D, GLYCEROL (3 entities in total) |
| 機能のキーワード | complement, c3, c3d, alpha-alpha barrel |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Secreted: P01024 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 33359.20 |
| 構造登録者 | Nagar, B.,Jones, R.G.,Diefenbach, R.J.,Isenman, D.E.,Rini, J.M. (登録日: 1998-05-19, 公開日: 1998-10-07, 最終更新日: 2024-10-16) |
| 主引用文献 | Nagar, B.,Jones, R.G.,Diefenbach, R.J.,Isenman, D.E.,Rini, J.M. X-ray crystal structure of C3d: a C3 fragment and ligand for complement receptor 2. Science, 280:1277-1281, 1998 Cited by PubMed Abstract: Activation and covalent attachment of complement component C3 to pathogens is the key step in complement-mediated host defense. Additionally, the antigen-bound C3d fragment interacts with complement receptor 2 (CR2; also known as CD21) on B cells and thereby contributes to the initiation of an acquired humoral response. The x-ray crystal structure of human C3d solved at 2.0 angstroms resolution reveals an alpha-alpha barrel with the residues responsible for thioester formation and covalent attachment at one end and an acidic pocket at the other. The structure supports a model whereby the transition of native C3 to its functionally active state involves the disruption of a complementary domain interface and provides insight into the basis for the interaction between C3d and CR2. PubMed: 9596584DOI: 10.1126/science.280.5367.1277 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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