Cited by 5,983SARS-CoV-2 and COVID-19 ResearchEnzyme Structure and FunctionAnimal Virus Infections Studies

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Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor

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Lan, Jun, Ge, Jiwan, Yu, Jinfang, Shan, Sisi, Zhou, Huan, Fan, Shilong, Zhang, Qi, Shi, Xuanling, Wang, Qisheng, Zhang, Linqi, Wang, Xinquan·2020·Nature

DOI 10.1038/s41586-020-2180-5

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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.

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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: Lan, Jun
Ge, Jiwan
Yu, Jinfang
Shan, Sisi
Zhou, Huan
Fan, Shilong
Zhang, Qi
Shi, Xuanling
Wang, Qisheng
Zhang, Linqi
Wang, Xinquan
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2020-03-30
Volume: 581
Issue: 7807
Pages: 215-220
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/s41586-020-2180-5
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
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
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

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Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor

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