Science· 2020Q1
Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2
- 5,603citations
- Q1SCImago
- 2020year
Short summary
Structures reveal how SARS-CoV-2 spike protein binds to human ACE2, suggesting two spike proteins can attach to an ACE2 dimer.
AI-generated from the title and abstract; the full text is not read.
Key points
- ACE2 forms a dimer when complexed with the membrane protein B0 AT1.
- The structure of the SARS-CoV-2 receptor binding domain interacting with ACE2 was determined.
- An ACE2 dimer can potentially bind two SARS-CoV-2 trimeric spike proteins.
- The structures provide a basis for developing therapeutics against SARS-CoV-2 entry.
AI-generated from the title and abstract; the full text is not read.
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
The authors' abstract, as published at the source. Science, 2020 · DOI ↗
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Field: Infectious Diseases
Infectious DiseasesMedicine