Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2

Corresponding author: Qiang Zhou

Affiliations: Key Laboratory of Structural Biology of Zhejiang Province, Institute of Biology, Westlake Institute for Advanced Study, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China; School of Life Sciences, Westlake University, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China; Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.

Publication date: this article was published online on March 27, 2020

DOI: 10.1126/science.abb2762

Highlights

The researchers present cryo–electron microscopy structures of full-length human ACE2 in the presence of the neutral amino acid transporter B0AT1 with or without the receptor binding domain (RBD) of the surface spike glycoprotein (S protein) of SARS-CoV-2, both at an overall resolution of 2.9 angstroms, with a local resolution of 3.5 angstroms at the ACE2-RBD interface. The ACE2-B0AT1 complex is assembled as a dimer of heterodimers, with the collectrin-like domain of ACE2 mediating homodimerization. The RBD is recognized by the extracellular peptidase domain of ACE2 mainly through polar residues.

Nomination Reasons

In this article, the authors showed how SARS-CoV-2 binds to human cells by revealing the high-resolution structure of full-length ACE2 in a dimeric assembly. The findings provide important insights into the molecular basis for coronavirus recognition and infection.

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