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

Corresponding authors: Linqi Zhang, Xinquan Wang

Affiliations: The Ministry of Education Key Laboratory of Protein Science, Beijing Advanced Innovation Center for Structural Biology, Beijing Frontier Research Center for Biological Structure, Collaborative Innovation Center for Biotherapy, School of Life Sciences, Tsinghua University, Beijing, China; Center for Global Health and Infectious Diseases, Comprehensive AIDS Research Center, Beijing Advanced Innovation Center for Structural Biology, School of Medicine, Tsinghua University, Beijing, China; Shanghai Synchrotron Radiation Facility, Shanghai Advanced Research Institute, Chinese Academy of Sciences, Shanghai, China.

Publication date: this article was published online on March 30, 2020

DOI: https://doi.org/10.1038/s41586-020-2180-5

Highlights

In this article, the researchers present the crystal structure of the 2019-nCoV spike receptor-binding domain (RBD) bound with the ACE2 receptor. They observed that 2019-nCoV RBD has almost the same overall structure and binding mode to ACE2 as SARS-CoV RBD. They further identified a few key amino acid residues in SARS-CoV-2 for the receptor interaction. The similarity in structure and sequence strongly indicate convergent evolution between the SARS-CoV-2 and SARS-CoV RBDs for improved binding to ACE2.

Nomination Reasons

By comparing the structures of SARS-CoV RBD and 2019-nCoV RBD, the researchers explained why two SARS-CoV antibodies could not neutralize SARS-CoV-2, which may shed insight on pan-coronavirus antibody development.

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