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

2020/03/04 by Renhong Yan, Yuanyuan Zhang, Yaning Li +3 · 14 citations
Medicine · Biochemistry, Genetics and Molecular Biology · #SARS-CoV-2 and COVID-19 Research #COVID-19 Clinical Research Studies #Receptor Mechanisms and Signaling

paper · pdf · doi:10.1126/science.abb2762

openalex publication_date 2020/03/04 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/31

Abstract

How SARS-CoV-2 binds to human cells Scientists are racing to learn the secrets of severe acute respiratory syndrome–coronavirus 2 (SARS-CoV-2), which is the cause of the pandemic disease COVID-19. The first step in viral entry is the binding of the viral trimeric spike protein to the human receptor angiotensin-converting enzyme 2 (ACE2). Yan et al. present the structure of human ACE2 in complex with a membrane protein that it chaperones, B 0 AT1. In the context of this complex, ACE2 is a dimer. A further structure shows how the receptor binding domain of SARS-CoV-2 interacts with ACE2 and suggests that it is possible that two trimeric spike proteins bind to an ACE2 dimer. The structures provide a basis for the development of therapeutics targeting this crucial interaction. Science , this issue p. 1444

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