Mar 7, 2020

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

Science
Renhong YanQiang Zhou

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.

Mentioned in this Paper

Local
EMILIN1 wt Allele
RNA Recognition Motif
Neutral Amino Acid Transporter A
ACE2 protein, human
SLC6A19
ACE2
Spike Glycoprotein, Coronavirus
N protein, Severe acute respiratory syndrome virus
SLC6A19 protein, human

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