The DOI matches its Crossref record; 37 of the 38 references it cites were found in a registry or an index.
Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor
Open accessPublished version of a preprint
Abstract
A new and highly pathogenic coronavirus (severe acute respiratory syndrome coronavirus-2, SARS-CoV-2) caused an outbreak in Wuhan city, Hubei province, China, starting from December 2019 that quickly spread nationwide and to other countries around the world 1-3. Here, to better understand the initial step of infection at an atomic level, we determined the crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 bound to the cell receptor ACE2. The overall ACE2-binding mode of the SARS-CoV-2 RBD is nearly identical to that of the SARS-CoV RBD, which also uses ACE2 as the cell receptor 4. Structural analysis identified residues in the SARS-CoV-2 RBD that are essential for ACE2 binding, the majority of which either are highly conserved or share similar side chain properties with those in the SARS-CoV RBD. Such similarity in structure and sequence strongly indicate convergent evolution between the SARS-CoV-2 and SARS-CoV RBDs for improved binding to ACE2, although SARS-CoV-2 does not cluster within SARS and SARS-related coronaviruses 1-3,5. The epitopes of two SARS-CoV antibodies that target the RBD are also analysed for binding to the SARS-CoV-2 RBD, providing insights into the future identification of cross-reactive antibodies.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“This amino acid sequence extends from residue Thr333 to residue Gly526 [28].”
From Effects of Mangiferin on LPS-Induced Inflammation and SARS-CoV-2 Viral Adsorption in Human Lung Cells (2022) · cites this paper as [28]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Importantly, ACE2 (angiotensin-converting enzyme 2) had been identified as the receptor for SARS-CoV 4,5 and SARS-CoV-2.”
From COVID-19, Myocarditis and Pericarditis (2023) · cites this paper as [7]
In the citing paper
“When binding to hACE2, spike amino acid F486 interacts with hACE2 residues L79, M82 and Y83, which collectively comprise a hotspot for ACE2 differences between mammalian species13.”
From Emergence of SARS-CoV-2 Omicron lineages BA.4 and BA.5 in South Africa (2022) · cites this paper as [13]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China
Huang, C., Wang, Y., Li, X., Ren, L., Zhao, J., Hu, Y., Zhang, L., Fan, G., Xu, J., Gu, X., et al. (2020) · The Lancet · doi:10.1016/s0140-6736(20)30183-5 · Cited by 48,884
Self-citation[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
A novel coronavirus from patients with pneumonia in China, 2019
Zhu, N., Zhang, D., Wang, W., Li, X., Yang, B., Song, J., Zhao, X., Huang, B., Shi, W., Lu, R., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2001017 · Cited by 28,244
A pneumonia outbreak associated with a new coronavirus of probable bat origin
Zhou, P., Yang, X.-L., Wang, X.-G., Hu, B., Zhang, L., Zhang, W., Si, H.-R., Zhu, Y., Li, B., Huang, C.-L., et al. (2020) · Nature · doi:10.1038/s41586-020-2012-7 · Cited by 21,969
Self-citationPhaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
Hoffmann, M., Kleine-Weber, H., Schroeder, S., Krüger, N., Herrler, T., Erichsen, S., Schiergens, T. S., Herrler, G., Wu, N.-H., Nitsche, A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.02.052 · Cited by 20,286
Wang, D., Hu, B., Hu, C., Zhu, F., Liu, X., Zhang, J., Wang, B., Xiang, H., Cheng, Z., Xiong, Y., et al. (2020) · JAMA · doi:10.1001/jama.2020.1585 · Cited by 20,148
Self-citationMartínez–González, M. B. (2020) · DSPACE System - Metalibrary (University of the Coast) · Cited by 18,292
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,961
Cited by
Sorted by citations
Items 1,001–1,026 of 1,026
Design Strategies for and Stability of mRNA–Lipid Nanoparticle COVID-19 Vaccines
Liu, T., Tian, Y., Zheng, A., & Cui, C. (2022) · Polymers · doi:10.3390/polym14194195 · Cited by 54
Circulating microRNAs as emerging regulators of COVID-19
Liang, Y., Fang, D., Gao, X., Deng, X., Chen, N., Wu, J., Min De, Z. E. N. G., & Luo, M. (2022) · Theranostics · doi:10.7150/thno.78164 · Cited by 54
Sharma, N., Modak, C., Singh, P. K., Kumar, R., Khatri, D. K., & Singh, S. B. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.02.090 · Cited by 54
The SARS-CoV-2 spike protein is vulnerable to moderate electric fields
Arbeitman, C. R., Rojas, P., Ojeda-May, P., & Garcia, M. E. (2021) · Nature Communications · doi:10.1038/s41467-021-25478-7 · Cited by 54
CAR-NK Cells Effectively Target SARS-CoV-2-Spike-Expressing Cell Lines In Vitro
Ma, M. T., Badeti, S., Chen, C.-H., Kim, J., Choudhary, A. K., Honnen, B., Reichman, C., Calianese, D. C., Pinter, A., Jiang, Q., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.652223 · Cited by 54
A scalable and highly immunogenic virus‐like particle‐based vaccine against SARS‐CoV‐2
Mohsen, M. O., Baļķe, I., Zinkhan, S., Zeltina, V., Liu, X., Chang, X., Krenger, P. S., Plattner, K., Gharailoo, Z., Vogt, A. S., et al. (2021) · Allergy · doi:10.1111/all.15080 · Cited by 54
Treatments Administered to the First 9152 Reported Cases of COVID-19: A Systematic Review
Fajgenbaum, D. C., Khor, J. S., Gorzewski, A., Tamakloe, M.-A., Powers, V., Kakkis, J. J., Repasky, M., Taylor, A., Beschloss, A., Hernandez-Miyares, L., et al. (2020) · Infectious Diseases and Therapy · doi:10.1007/s40121-020-00303-8 · Cited by 52
COVID-19 as a trigger for type 1 diabetes
Wang, Y., Guo, H., Wang, G., Zhai, J., & Du, B. (2023) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgad165 · Cited by 50
Deng, P., Ke, Z., Ying, B., Qiao, B., & Yuan, L. (2020) · Clinica Chimica Acta · doi:10.1016/j.cca.2020.07.018 · Cited by 47
DNA damage response at telomeres boosts the transcription of SARS‐CoV‐2 receptor ACE2 during aging
Sepe, S., Rossiello, F., Cancila, V., Iannelli, F., Matti, V., Cicio, G., Cabrini, M., Marinelli, E., Alabi, B. R., di Lillo, A., et al. (2022) · The EMBO Reports · doi:10.15252/embr.202153658 · Cited by 42
Cong, Y., Feng, Y., Ni, H., Zhi, F., Miao, Y., Fang, B., Zhang, L., & Zhang, J. Z. H. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c00241 · Cited by 40
Self-citationGlobal Diversification and Distribution of Coronaviruses With Furin Cleavage Sites
Liu, X., Wu, Q., & Zhang, Z. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.649314 · Cited by 32
Free energy perturbation calculations of mutation effects on SARS-CoV-2 RBD::ACE2 binding affinity
Sergeeva, A. P., Katsamba, P. S., Liao, J., Sampson, J. M., Bahna, F., Mannepalli, S., Morano, N. C., Shapiro, L., Friesner, R. A., & Honig, B. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168187 · Cited by 27
Kim, J., Mukherjee, A., Nelson, D., Jozic, A., & Sahay, G. (2020) · doi:10.1101/2020.07.24.205583 · Cited by 28
Hazardous Shortcuts in Standard Binding Free Energy Calculations
Blazhynska, M., Goulard Coderc de Lacam, E., Chen, H., Roux, B., & Chipot, C. (2022) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.2c01490 · Cited by 27
Lubin, J. H., Markosian, C., Balamurugan, D., Ma, M. T., Chen, C.-H., Liu, D., Pasqualini, R., Arap, W., Burley, S. K., & Khare, S. D. (2023) · JCI Insight · doi:10.1172/jci.insight.168296 · Cited by 26
Yantiss, R. K., Qin, L., He, B., Crawford, C. V., Seshan, S., Patel, S., Wahid, N., & Jessurun, J. (2022) · American Journal of Surgical Pathology · doi:10.1097/pas.0000000000001755 · Cited by 23
Dudas, G., Hong, S. L., Potter, B., Calvignac-Spencer, S., Niatou-Singa, F. S., Tombolomako, T. B., Fuh-Neba, T., Vickos, U., Ulrich, M., Leendertz, F. H., et al. (2021) · doi:10.1101/2021.05.04.21256637 · Cited by 76
A Potent and Protective Human Neutralizing Antibody Against SARS-CoV-2 Variants
Shan, S., Mok, C. K., Zhang, S., Lan, J., Li, J., Yang, Z., Wang, R., Cheng, L., Fang, M., Aw, Z. Q., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.766821 · Cited by 21
Self-citationDevaux, C. A., & Camoin-Jau, L. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.1042200 · Cited by 20
Chen, H., Peng, J., Wang, T., Wen, J., Chen, S., Huang, Y., & Zhang, Y. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115370 · Cited by 19
Beyond dexamethasone, emerging immuno‐thrombotic therapies for COVID‐19
Jensen, M. P., George, M., Gilroy, D., & Sofat, R. (2021) · British Journal of Clinical Pharmacology · doi:10.1111/bcp.14540 · Cited by 17
Spampinato, M., Carota, G., Sferrazzo, G., Fuochi, V., Distefano, A., Ronsisvalle, S., Sipala, F., Giuffrida, R., Furneri, P. M., Di Rosa, M., et al. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14122845 · Cited by 14
“This amino acid sequence extends from residue Thr333 to residue Gly526 [28].”
BackgroundMunawaroh, H. S. H., Gumilar, G. G., Pratiwi, R. N., Khoiriah, S. F., Ningrum, A., Martha, L., Chew, K. W., & Show, P.-L. (2024) · Algal Research · doi:10.1016/j.algal.2024.103468 · Cited by 9
Kadam, V., Bhargav, P., & Mukherjee, A. (2026) · Journal of Chemical Sciences · doi:10.1007/s12039-025-02459-7
Metadata
- Authors
- Lan, J., Ge, J., Yu, J., Shan, S., Zhou, H., Fan, S., Zhang, Q., Shi, X., Wang, Q., Zhang, L., & Wang, X.
- Affiliations
- Tsinghua University (CN)
- Chinese Academy of Sciences (CN)
- Corresponding author
- Zhang, Qi
- Zhang, Linqi
- Wang, Xinquan
- ORCID
- Venue
- Nature
- Published
- 2020-03-30
- Volume
- 581
- Issue
- 7807
- Pages
- 215-220
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W3014067025
- Cited by
- 5,983
- References
- 38
- Citations by year
- 2026: 207 · 2025: 404 · 2024: 573 · 2023: 797 · 2022: 1237 · 2021: 1678 · 2020: 1076
- FWCI
- 152.41
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Nature (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Salt Science Research Foundation
- Tencent
- Tsinghua University (20201080053)
- Beijing Municipal Science and Technology Commission (171100000517-001 and -003)
- Beijing Advanced Innovation Center for Structural Biology, Tsinghua University
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Keywords
- SARS-CoV-2, spike protein, receptor binding domain, ACE2, crystal structure, SARS-CoV, convergent evolution, antibody epitopes, cross-reactive antibodies, viral entry, binding site residues
- MeSH terms
- Protein Domains, Betacoronavirus, Angiotensin-Converting Enzyme 2, SARS-CoV-2, Amino Acid Sequence, Epitopes, Binding Sites, Humans, Hydrogen Bonding, Peptidyl-Dipeptidase A, Models, Molecular, Protein Binding, Receptors, Virus, Salts, Water, Sequence Alignment, Conserved Sequence, Crystallography, X-Ray, Evolution, Molecular, Severe acute respiratory syndrome-related coronavirus, Antibodies, Neutralizing, Spike Glycoprotein, Coronavirus
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
