7MF1
Crystal structure of SARS-CoV-2 receptor binding domain in complex with neutralizing antibody 47D1
7MF1 の概要
| エントリーDOI | 10.2210/pdb7mf1/pdb |
| 分子名称 | Spike protein S1, 47D1 Fab heavy chain, 47D1 Fab light chain, ... (6 entities in total) |
| 機能のキーワード | covid-19, immune system-viral protein complex, immune system/viral protein |
| 由来する生物種 | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2) 詳細 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 71136.23 |
| 構造登録者 | |
| 主引用文献 | Zhou, X.,Ma, F.,Xie, J.,Yuan, M.,Li, Y.,Shaabani, N.,Zhao, F.,Huang, D.,Wu, N.C.,Lee, C.D.,Liu, H.,Li, J.,Chen, Z.,Hong, Y.,Liu, W.H.,Xiao, N.,Burton, D.R.,Tu, H.,Li, H.,Chen, X.,Teijaro, J.R.,Wilson, I.A.,Xiao, C.,Huang, Z. Diverse immunoglobulin gene usage and convergent epitope targeting in neutralizing antibody responses to SARS-CoV-2. Cell Rep, 35:109109-109109, 2021 Cited by PubMed Abstract: It is unclear whether individuals with enormous diversity in B cell receptor repertoires are consistently able to mount effective antibody responses against SARS-CoV-2. We analyzed antibody responses in a cohort of 55 convalescent patients and isolated 54 potent neutralizing monoclonal antibodies (mAbs). While most of the mAbs target the angiotensin-converting enzyme 2 (ACE2) binding surface on the receptor binding domain (RBD) of SARS-CoV-2 spike protein, mAb 47D1 binds only to one side of the receptor binding surface on the RBD. Neutralization by 47D1 is achieved independent of interfering RBD-ACE2 binding. A crystal structure of the mAb-RBD complex shows that the IF motif at the tip of 47D1 CDR H2 interacts with a hydrophobic pocket in the RBD. Diverse immunoglobulin gene usage and convergent epitope targeting characterize neutralizing antibody responses to SARS-CoV-2, suggesting that vaccines that effectively present the receptor binding site on the RBD will likely elicit neutralizing antibody responses in a large fraction of the population. PubMed: 33932326DOI: 10.1016/j.celrep.2021.109109 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.092 Å) |
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