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7TCC

Cryo-EM structure of SARS-CoV-2 Omicron spike in complex with antibodies A19-46.1 and B1-182.1

7TCC の概要
エントリーDOI10.2210/pdb7tcc/pdb
EMDBエントリー25808
分子名称Spike glycoprotein, Heavy chain of antibody A19-46.1, Light chain of antibody A19-46.1, ... (7 entities in total)
機能のキーワードsars-cov-2, spike, antibody, viral protein, viral protein-immune system complex, viral protein/immune system
由来する生物種Severe acute respiratory syndrome coronavirus 2
詳細
タンパク質・核酸の鎖数15
化学式量合計584510.56
構造登録者
Zhou, T.,Kwong, P.D. (登録日: 2021-12-23, 公開日: 2022-03-30, 最終更新日: 2024-10-23)
主引用文献Zhou, T.,Wang, L.,Misasi, J.,Pegu, A.,Zhang, Y.,Harris, D.R.,Olia, A.S.,Talana, C.A.,Yang, E.S.,Chen, M.,Choe, M.,Shi, W.,Teng, I.T.,Creanga, A.,Jenkins, C.,Leung, K.,Liu, T.,Stancofski, E.D.,Stephens, T.,Zhang, B.,Tsybovsky, Y.,Graham, B.S.,Mascola, J.R.,Sullivan, N.J.,Kwong, P.D.
Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529.
Science, 376:eabn8897-eabn8897, 2022
Cited by
PubMed Abstract: The rapid spread of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) B.1.1.529 (Omicron) variant and its resistance to neutralization by vaccinee and convalescent sera are driving a search for monoclonal antibodies with potent neutralization. To provide insight into effective neutralization, we determined cryo-electron microscopy structures and evaluated receptor binding domain (RBD) antibodies for their ability to bind and neutralize B.1.1.529. Mutations altered 16% of the B.1.1.529 RBD surface, clustered on an RBD ridge overlapping the angiotensin-converting enzyme 2 (ACE2)-binding surface and reduced binding of most antibodies. Substantial inhibitory activity was retained by select monoclonal antibodies-including A23-58.1, B1-182.1, COV2-2196, S2E12, A19-46.1, S309, and LY-CoV1404-that accommodated these changes and neutralized B.1.1.529. We identified combinations of antibodies with synergistic neutralization. The analysis revealed structural mechanisms for maintenance of potent neutralization against emerging variants.
PubMed: 35324257
DOI: 10.1126/science.abn8897
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.86 Å)
構造検証レポート
Validation report summary of 7tcc
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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