Structure of Coronavirus Receptor on Human Cells Determined

  • Author:
  • Published: 06 March 2020
  • Copyright: Wiley-VCH Verlag GmbH & Co. KGaA
  • Source / Publisher: Science/American Association for the Advancement of Science
thumbnail image: Structure of Coronavirus Receptor on Human Cells Determined

Coronaviruses have glycoprotein "spikes" on their surface, which help the virus to enter host cells by fusing the virus and the cell membrane. The structure of the spike protein of the coronavirus SARS-CoV-2 that causes the current outbreak of COVID-19 has recently been determined by cryogenic electron microscopy (cryo-EM). Cryo-EM uses very low temperatures to allow the determination of biomolecular structures at almost atomic resolution.

The coronavirus spike contains a receptor-binding domain (RBD) subunit, which binds to a receptor on the surface of the host cells' membrane—the angiotensin-converting enzyme 2 (ACE2). However, the full-length structure of ACE2 has been difficult to determine so far.

Qiang Zhou, Key Westlake Institute for Advanced Study and Westlake University, both, Hangzhou, China, have obtained cryo-EM structures of full-length human ACE2. The measurements were performed in the presence of the neutral amino acid transporter B0AT1, which provides stabilization. The structures were recorded both with and without the RBD of the spike protein of SARS-CoV-2. The team co-expressed the ACE2 and B0AT1 proteins in a human cell line, mixed a part of the samples with RBD, and studied the resulting complexes using cryo-EM. The structures have an overall resolution of 2.9 Å and a local resolution of 3.5 Å at the ACE2–RBD interface.

The researchers found that the ACE2–B0AT1 complex has a dimeric structure, with the ACE2 dimer sandwiched by B0AT1. Overall, ACE2 consists of a peptidase domain (PD) on the outer side of the cell membrane and a collectrin-like domain (CLD) that ends with a single transmembrane helix and an intracellular segment. The structure of the ternary RBD–ACE2–B0AT1 complex shows that each PD binds to one RBD, mainly via polar interactions. This is similar to the interaction between the SARS virus and ACE2. According to the team, these results could be helpful for the structure-based design of compounds that bind to either ACE2 or the spike protein of coronaviruses and, thus, suppress viral infection.

Also of Interest


  • LitCovid
    Curated literature hub for tracking up-to-date scientific information about COVID-19
  • Many publishers and other entities have signed a joint statement to ensure that COVID-19 research findings and data are shared rapidly and openly



Article Views: 3644

Sign in Area

Please sign in below

Additional Sign In options

Please note that to comment on an article you must be registered and logged in.
Registration is for free, you may already be registered to receive, e.g., the newsletter. When you register on this website, please ensure you view our terms and conditions. All comments are subject to moderation.

Article Comments - To add a comment please sign in

If you would like to reuse any content, in print or online, from, please contact us first for permission. more

Follow on Facebook Follow on Twitter Follow on YouTube Follow on LinkedIn Follow on Instagram RSS Sign up for newsletters

Magazine of Chemistry Europe (16 European Chemical Societies) published by Wiley-VCH