S373P Mutation Stabilizes the Receptor-Binding Domain of the Spike Protein in Omicron and Promotes Binding-Reference-Cited by-同舟云学术

S373P Mutation Stabilizes the Receptor-Binding Domain of the Spike Protein in Omicron and Promotes Binding

Published:2023-06-22 Issue:7 Volume:3 Page:1902-1910
ISSN:2691-3704
Container-title:JACS Au
language:en
Short-container-title:JACS Au

Author:

Zheng Bin¹,Xiao Yuelong¹,Tong Bei²,Mao Yutong¹,Ge Rui¹,Tian Fang¹,Dong Xianchi³⁴,Zheng Peng¹^ORCID

Affiliation:

1. State Key Laboratory of Coordination Chemistry, Chemistry and Biomedicine Innovation Center (ChemBIC), School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, Jiangsu 210023, China

2. Institute of Botany, Jiangsu Province and Chinese Academy of Sciences, Nanjing, Jiangsu 210014, China

3. State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing University, Nanjing, Jiangsu 210023, China

4. Engineering Research Center of Protein and Peptide Medicine, Ministry of Education, Nanjing, Jiangsu 210023, China

Funder

Natural Science Foundation of Jiangsu Province

Fundamental Research Funds for the Central Universities

National Natural Science Foundation of China

Publisher

American Chemical Society (ACS)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Chemistry (miscellaneous),Analytical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jacsau.3c00142

Reference55 articles.

1. Structure, Function, and Evolution of Coronavirus Spike Proteins

2. A new coronavirus associated with human respiratory disease in China

3. Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor

4. A Novel Coronavirus Associated with Severe Acute Respiratory Syndrome

5. Deep Mutational Scanning of SARS-CoV-2 Receptor Binding Domain Reveals Constraints on Folding and ACE2 Binding

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