4W4O
High-resolution crystal structure of Fc bound to its human receptor Fc-gamma-RI
4W4O の概要
| エントリーDOI | 10.2210/pdb4w4o/pdb |
| 関連するPDBエントリー | 4W4N |
| 分子名称 | Ig gamma-1 chain C region, High affinity immunoglobulin gamma Fc receptor I, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total) |
| 機能のキーワード | immune complex igg1 protein-protein complex asymmetry, immune system |
| 由来する生物種 | Homo sapiens (Human) 詳細 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 87850.19 |
| 構造登録者 | |
| 主引用文献 | Kiyoshi, M.,Caaveiro, J.M.M.,Kawai, T.,Tashiro, S.,Ide, T.,Asaoka, Y.,Hatayama, K.,Tsumoto, K. Structural basis for binding of human IgG1 to its high-affinity human receptor Fc gamma RI Nat Commun, 6:6866-6866, 2015 Cited by PubMed Abstract: Cell-surface Fcγ receptors mediate innate and adaptive immune responses. Human Fcγ receptor I (hFcγRI) binds IgGs with high affinity and is the only Fcγ receptor that can effectively capture monomeric IgGs. However, the molecular basis of hFcγRI's interaction with Fc has not been determined, limiting our understanding of this major immune receptor. Here we report the crystal structure of a complex between hFcγRI and human Fc, at 1.80 Å resolution, revealing an unique hydrophobic pocket at the surface of hFcγRI perfectly suited for residue Leu235 of Fc, which explains the high affinity of this complex. Structural, kinetic and thermodynamic data demonstrate that the binding mechanism is governed by a combination of non-covalent interactions, bridging water molecules and the dynamic features of Fc. In addition, the hinge region of hFcγRI-bound Fc adopts a straight conformation, potentially orienting the Fab moiety. These findings will stimulate the development of novel therapeutic strategies involving hFcγRI. PubMed: 25925696DOI: 10.1038/ncomms7866 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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