6XC3

Crystal structure of SARS-CoV-2 receptor binding domain in complex with antibodies CC12.1 and CR3022

6XC3 の概要

• エントリーDOI: 10.2210/pdb6xc3/pdb
• 関連するPDBエントリー: 6XC2
• 分子名称: CR3022 heavy chain, CR3022 light chain, CC12.1 light chain, ... (7 entities in total)
• 機能のキーワード: antibody, sars-cov-2, coronavirus, spike, immune system, immune system-viral protein complex, immune system/viral protein
• 由来する生物種: Homo sapiens; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 121144.41

構造登録者

Yuan, M.,Liu, H.,Wu, N.C.,Zhu, X.,Wilson, I.A. (登録日: 2020-06-08, 公開日: 2020-07-08, 最終更新日: 2024-11-20)

主引用文献

Yuan, M.,Liu, H.,Wu, N.C.,Lee, C.D.,Zhu, X.,Zhao, F.,Huang, D.,Yu, W.,Hua, Y.,Tien, H.,Rogers, T.F.,Landais, E.,Sok, D.,Jardine, J.G.,Burton, D.R.,Wilson, I.A.
Structural basis of a shared antibody response to SARS-CoV-2.
Science, 369:1119-1123, 2020

PubMed Abstract: Molecular understanding of neutralizing antibody responses to severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) could accelerate vaccine design and drug discovery. We analyzed 294 anti-SARS-CoV-2 antibodies and found that immunoglobulin G heavy-chain variable region 3-53 (IGHV3-53) is the most frequently used IGHV gene for targeting the receptor-binding domain (RBD) of the spike protein. Co-crystal structures of two IGHV3-53-neutralizing antibodies with RBD, with or without Fab CR3022, at 2.33- to 3.20-angstrom resolution revealed that the germline-encoded residues dominate recognition of the angiotensin I converting enzyme 2 (ACE2)-binding site. This binding mode limits the IGHV3-53 antibodies to short complementarity-determining region H3 loops but accommodates light-chain diversity. These IGHV3-53 antibodies show minimal affinity maturation and high potency, which is promising for vaccine design. Knowledge of these structural motifs and binding mode should facilitate the design of antigens that elicit this type of neutralizing response.

PubMed: 32661058
DOI: 10.1126/science.abd2321

実験手法

X-RAY DIFFRACTION (2.698 Å)