Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural basis for bivalent binding and inhibition of SARS-CoV-2 infection by human potent neutralizing antibodies.
Journal, issue, pages	Cell Res, Vol. 31, Issue 5, Page 517-525, Year 2021
Publish date	Mar 17, 2021
Authors	Renhong Yan / Ruoke Wang / Bin Ju / Jinfang Yu / Yuanyuan Zhang / Nan Liu / Jia Wang / Qi Zhang / Peng Chen / Bing Zhou / Yaning Li / Yaping Shen / Shuyuan Zhang / Long Tian / Yingying Guo / Lu Xia / Xinyue Zhong / Lin Cheng / Xiangyang Ge / Juanjuan Zhao / Hong-Wei Wang / Xinquan Wang / Zheng Zhang / Linqi Zhang / Qiang Zhou /
PubMed Abstract	Neutralizing monoclonal antibodies (nAbs) to severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) represent promising candidates for clinical intervention against coronavirus disease 2019 ...Neutralizing monoclonal antibodies (nAbs) to severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) represent promising candidates for clinical intervention against coronavirus disease 2019 (COVID-19). We isolated a large number of nAbs from SARS-CoV-2-infected individuals capable of disrupting proper interaction between the receptor binding domain (RBD) of the viral spike (S) protein and the receptor angiotensin converting enzyme 2 (ACE2). However, the structural basis for their potent neutralizing activity remains unclear. Here, we report cryo-EM structures of the ten most potent nAbs in their native full-length IgG-form or in both IgG-form and Fab-form bound to the trimeric S protein of SARS-CoV-2. The bivalent binding of the full-length IgG is found to associate with more RBDs in the "up" conformation than the monovalent binding of Fab, perhaps contributing to the enhanced neutralizing activity of IgG and triggering more shedding of the S1 subunit from the S protein. Comparison of a large number of nAbs identified common and unique structural features associated with their potent neutralizing activities. This work provides a structural basis for further understanding the mechanism of nAbs, especially through revealing the bivalent binding and its correlation with more potent neutralization and the shedding of S1 subunit.
External links	Cell Res / PubMed:33731853 / PubMed Central
Methods	EM (single particle)
Resolution	2.7 - 7.3 Å
Structure data	30512 7czp EMDB-30512, PDB-7czp: S protein of SARS-CoV-2 in complex bound with P2B-1A1 Method: EM (single particle) / Resolution: 3.0 Å 30513 7czq EMDB-30513: cryo EM map of the S protein of SARS-CoV-2 in complex bound with P2B-1A10 PDB-7czq: S protein of SARS-CoV-2 in complex bound with P2B-1A10 Method: EM (single particle) / Resolution: 2.8 Å 30514 7czr EMDB-30514, PDB-7czr: S protein of SARS-CoV-2 in complex bound with P5A-1B8_2B Method: EM (single particle) / Resolution: 3.5 Å 30515 7czs EMDB-30515, PDB-7czs: S protein of SARS-CoV-2 in complex bound with P5A-1B8_3B Method: EM (single particle) / Resolution: 3.6 Å 30516 7czt EMDB-30516, PDB-7czt: S protein of SARS-CoV-2 in complex bound with P5A-2G9 Method: EM (single particle) / Resolution: 2.7 Å 30517 7czu EMDB-30517, PDB-7czu: S protein of SARS-CoV-2 in complex bound with P5A-1B6_2B Method: EM (single particle) / Resolution: 3.4 Å 30518 7czv EMDB-30518, PDB-7czv: S protein of SARS-CoV-2 in complex bound with P5A-1B6_3B Method: EM (single particle) / Resolution: 3.3 Å 30519 7czw EMDB-30519, PDB-7czw: S protein of SARS-CoV-2 in complex bound with P5A-2G7 Method: EM (single particle) / Resolution: 2.8 Å 30520 7czx EMDB-30520, PDB-7czx: S protein of SARS-CoV-2 in complex bound with P5A-1B9 Method: EM (single particle) / Resolution: 2.8 Å 30521 7czy EMDB-30521, PDB-7czy: S protein of SARS-CoV-2 in complex bound with P5A-2F11_2B Method: EM (single particle) / Resolution: 3.3 Å 30522 7czz EMDB-30522, PDB-7czz: S protein of SARS-CoV-2 in complex bound with P5A-2F11_3B Method: EM (single particle) / Resolution: 3.2 Å 30523 7d00 EMDB-30523, PDB-7d00: S protein of SARS-CoV-2 in complex bound with FabP5A-1B8 Method: EM (single particle) / Resolution: 3.0 Å 30524 7d03 EMDB-30524, PDB-7d03: S protein of SARS-CoV-2 in complex bound with FabP5A-2G7 Method: EM (single particle) / Resolution: 3.2 Å 30529 7d0b EMDB-30529, PDB-7d0b: S protein of SARS-CoV-2 in complex bound with P5A-3C12_1B Method: EM (single particle) / Resolution: 3.9 Å 30530 7d0c EMDB-30530, PDB-7d0c: S protein of SARS-CoV-2 in complex bound with P5A-3A1 Method: EM (single particle) / Resolution: 3.4 Å 30531 7d0d EMDB-30531, PDB-7d0d: S protein of SARS-CoV-2 in complex bound with P5A-3C12_2B Method: EM (single particle) / Resolution: 3.8 Å EMDB-30871: Re-centered cryo EM map of the S protein of SARS-CoV-2 in complex bound with P5A-1B8 Method: EM (single particle) / Resolution: 4.7 Å EMDB-30872: Re-centered cryo EM map of the S protein of SARS-CoV-2 in complex bound with FabP5A-1B8 Method: EM (single particle) / Resolution: 6.7 Å EMDB-30873: Re-centered cryo EM map of the S protein of SARS-CoV-2 in complex bound with P5A-2G7 Method: EM (single particle) / Resolution: 4.7 Å EMDB-30874: Re-centered cryo EM map of the S protein of SARS-CoV-2 in complex bound with FabP5A-2G7 Method: EM (single particle) / Resolution: 7.3 Å
Chemicals	ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine
Source	homo sapiens (human) severe acute respiratory syndrome coronavirus 2
Keywords	VIRAL PROTEIN / SARS-CoV-2 / antibody / VIRAL PROTEIN/IMMUNE SYSTEM / Spike / IMMUNE SYSTEM / VIRAL PROTEIN-IMMUNE SYSTEM complex