Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2
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Open Access
- 27 March 2020
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 367 (6485), 1444-1448
- https://doi.org/10.1126/science.abb2762
Abstract
Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for SARS coronavirus (SARS-CoV) and the new coronavirus (SARS-CoV-2) that is causing the serious epidemic COVID-19. Here we present cryo-EM structures of full-length human ACE2, in the presence of a 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 Å, with a local resolution of 3.5 Å at the ACE2-RBD interface. The ACE2-B0AT1 complex is assembled as a dimer of heterodimers, with the Collectrin-like domain (CLD) of ACE2 mediating homo-dimerization. The RBD is recognized by the extracellular peptidase domain (PD) of ACE2 mainly through polar residues. These findings provide important insights to the molecular basis for coronavirus recognition and infection.Keywords
Funding Information
- National Natural Science Foundation of China (31971123)
- National Natural Science Foundation of China (81920108015)
- National Natural Science Foundation of China (31930059)
- Key R&D Program of Zhejiang Province (2020C04001)
- the SARS-CoV-2 emergency project of the Science and Technology Department of Zhejiang Province (2020C03129)
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