4YPG
Structural Insights Into the Neutralization Properties of a Human Anti-Interferon Monoclonal Antibody
4YPG の概要
エントリーDOI | 10.2210/pdb4ypg/pdb |
分子名称 | Sifalimumab light chain, Sifalimumab heavy chain, Interferon alpha-2, ... (5 entities in total) |
機能のキーワード | therapeutic mab, ifn-alpha2a, immune system |
由来する生物種 | Homo sapiens (Human) 詳細 |
タンパク質・核酸の鎖数 | 6 |
化学式量合計 | 131149.01 |
構造登録者 | |
主引用文献 | Oganesyan, V.,Peng, L.,Woods, R.M.,Wu, H.,Dall'Acqua, W.F. Structural Insights into the Neutralization Properties of the Fully Human, Anti-interferon Monoclonal Antibody Sifalimumab. J.Biol.Chem., 290:14979-14985, 2015 Cited by PubMed Abstract: We report the three-dimensional structure of human interferon α-2A (IFN-α2A) bound to the Fab fragment of a therapeutic monoclonal antibody (sifalimumab; IgG1/κ). The structure of the corresponding complex was solved at a resolution of 3.0 Å using molecular replacement and constitutes the first reported structure of a human type I IFN bound to a therapeutic antibody. This study revealed the major contribution made by the first complementarity-determining region in each of sifalimumab light and heavy chains. These data also provided the molecular basis for sifalimumab mechanism of action. We propose that its interferon-neutralizing properties are the result of direct competition for IFN-α2A binding to the IFN receptor subunit 1 (IFNAR1) and do not involve inhibiting IFN-α2A binding to the IFN receptor subunit 2 (IFNAR2). PubMed: 25925951DOI: 10.1074/jbc.M115.652156 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3 Å) |
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