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

Explore this paper's citation graph

Summary

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 of SARS-CoV-2 are presented, providing important insights into the molecular basis for coronavirus recognition and infection.

Type
article
Published
2020-03-04
Cited by
4,545
References
53
Access
Open access

Keywords

Coronavirus, Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), Angiotensin-converting enzyme 2, Extracellular, Angstrom

References

Cited by

Related papers