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

• Published in: Science (American Association for the Advancement of Science) Vol. 367; no. 6485; pp. 1444 - 1448
• Main Authors: Yan, Renhong, Zhang, Yuanyuan, Li, Yaning, Xia, Lu, Guo, Yingying, Zhou, Qiang
• Format: Journal Article
• Language: English
• Published: United States The American Association for the Advancement of Science 27.03.2020; American Association for the Advancement of Science
• Subjects: ACE2; Amino Acid Sequence; Amino Acid Transport Systems, Neutral - ultrastructure; Amino acids; Angiotensin; Angiotensin-Converting Enzyme 2; Betacoronavirus; Binding; Biochem; Cell Biol; Chaperones; Coronaviridae; Coronavirus Infections; Coronaviruses; COVID-19; Cryoelectron Microscopy; Dimers; Domains; Drug development; Electron microscopy; Enzymes; Glycoproteins; Humans; Membrane proteins; Models, Molecular; Molecular structure; Pandemics; Peptidase; Peptidyl-Dipeptidase A - ultrastructure; Pneumonia, Viral; Protein Binding; Protein Domains; Protein Multimerization; Proteins; Racing; Receptors, Virus - ultrastructure; Recognition; Respiratory diseases; SARS Virus; SARS-CoV-2; Sequence Alignment; Severe acute respiratory syndrome; Severe acute respiratory syndrome coronavirus 2; Spike glycoprotein; Spike Glycoprotein, Coronavirus - ultrastructure; Spike protein; Viral diseases

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-len...