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6XC7

Crystal structure of SARS-CoV-2 receptor binding domain in complex with antibodies CC12.3 and CR3022

Summary for 6XC7
Entry DOI10.2210/pdb6xc7/pdb
Related6XC2 6XC3 6XC4
DescriptorSpike protein S1, CR3022 heavy chain, CR3022 light chain, ... (6 entities in total)
Functional Keywordsantibody, sars-cov-2, coronavirus, spike, immune system, immune system-viral protein complex, immune system/viral protein
Biological sourceSevere acute respiratory syndrome coronavirus 2 (2019-nCoV)
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Total number of polymer chains5
Total formula weight121323.39
Authors
Yuan, M.,Liu, H.,Wu, N.C.,Zhu, X.,Wilson, I.A. (deposition date: 2020-06-08, release date: 2020-07-08, Last modification date: 2024-10-23)
Primary citationYuan, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.883 Å)
Structure validation

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