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

Author:

Yan Renhong12ORCID,Zhang Yuanyuan12ORCID,Li Yaning3,Xia Lu12ORCID,Guo Yingying12,Zhou Qiang12ORCID

Affiliation:

1. Key Laboratory of Structural Biology of Zhejiang Province, Institute of Biology, Westlake Institute for Advanced Study, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China.

2. School of Life Sciences, Westlake University, 18 Shilongshan Road, Hangzhou 310024, Zhejiang Province, China.

3. Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.

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

Funder

National Natural Science Foundation of China

Key R&D Program of Zhejiang Province

the SARS-CoV-2 emergency project of the Science and Technology Department of Zhejiang Province

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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