Structural basis for the different states of the spike protein of SARS-CoV-2 in complex with ACE2
Dear Editor,
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)has become a severe threat to global health.1 The spike (S) protein on the surface of SARS-CoV-2 exploits angiotensin-converting enzyme 2 (ACE2) as cellular receptor and mediates the fusion of the viral and the host cell membrane during infection.1,2 The activation of the S protein requires the receptor-binding domain(RBD) binding to the peptidase domain (PD) of ACE2 and the cleavage by host proteases into the N-terminal S1 subunit and the C-terminal S2 subunit.2-4 An additional furin cleavage site "RRAR"present in the S1/S2 cleavage region of SARS-CoV-2,which is absent in SARS-CoV that shares about 80％ sequence identity with SARS-CoV-2 and caused an epidemic in 2002-2003,might help accelerate the activation of the S protein.S1 consists of the N-terminal domain (NTD),the RBD,subdomain 1 and 2 (SD1 andSD2).
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We thank the cryo-EM facility,the high-performance computing center and the mass spectrometry & metabolomics core facility of Westlake University for providing supports;This work was funded by the National Natural Science Foundation of China;the SARS-CoV-2 emer-gency project of the Science and Technology Department of Zhejiang Province;the Key R&D Program of Zhejiang Province ;the China Postdoctoral Science Foundation ;the National Postdoctoral Program for Innovative Talents of China ;the Leading Innovative and Entrepreneur Team Introduction Program of Hangzhou,Westlake Education Foundation and Tencent Foundation
2021-07-12（万方平台首次上网日期，不代表论文的发表时间）
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717-719
