Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 32132184.
- Also identified by DOI 10.1126/science.abb2762 and PMC identifier 7164635.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for severe acute respiratory syndrome-coronavirus (SARS-CoV) and the new coronavirus (SARS-CoV-2) that is causing the serious coronavirus disease 2019 (COVID-19) epidemic. Here, we present cryo-electron microscopy structures of full-length human ACE2 in the presence of the neutral amino acid transporter B<sup>0</sup>AT1 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-B<sup>0</sup>AT1 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. These findings provide important insights into the molecular basis for coronavirus recognition and infection.
Medical subject headings
- Amino Acid Transport Systems, Neutral
- Peptidyl-Dipeptidase A
- Receptors, Virus
- Spike Glycoprotein, Coronavirus