7TLZ
SARS-CoV-2 S NTD B.1.1.529 Omicron variant + S309 Local Refinement
7TLZ の概要
| エントリーDOI | 10.2210/pdb7tlz/pdb |
| 関連するPDBエントリー | 7TLY 7TLZ 7TM0 7TN0 |
| EMDBエントリー | 25990 25991 25992 25993 |
| 分子名称 | S2L20 Fab light chain, S2L20 Fab heavy chain, Spike glycoprotein, ... (4 entities in total) |
| 機能のキーワード | omicron, receptor-binding domain, sars-cov-2, covid, b.1.529, ntd, antibody, fab, s2l20, structural genomics, seattle structural genomics center for infectious disease, ssgcid, virus-immune system complex, virus/immune system |
| 由来する生物種 | Homo sapiens 詳細 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 168297.75 |
| 構造登録者 | McCallum, M.,Veesler, D.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2022-01-19, 公開日: 2022-02-02, 最終更新日: 2024-11-13) |
| 主引用文献 | McCallum, M.,Czudnochowski, N.,Rosen, L.E.,Zepeda, S.K.,Bowen, J.E.,Walls, A.C.,Hauser, K.,Joshi, A.,Stewart, C.,Dillen, J.R.,Powell, A.E.,Croll, T.I.,Nix, J.,Virgin, H.W.,Corti, D.,Snell, G.,Veesler, D. Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement. Science, 375:864-868, 2022 Cited by PubMed Abstract: The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron variant of concern evades antibody-mediated immunity that comes from vaccination or infection with earlier variants due to accumulation of numerous spike mutations. To understand the Omicron antigenic shift, we determined cryo-electron microscopy and x-ray crystal structures of the spike protein and the receptor-binding domain bound to the broadly neutralizing sarbecovirus monoclonal antibody (mAb) S309 (the parent mAb of sotrovimab) and to the human ACE2 receptor. We provide a blueprint for understanding the marked reduction of binding of other therapeutic mAbs that leads to dampened neutralizing activity. Remodeling of interactions between the Omicron receptor-binding domain and human ACE2 likely explains the enhanced affinity for the host receptor relative to the ancestral virus. PubMed: 35076256DOI: 10.1126/science.abn8652 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.3 Å) |
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