Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor.
Jun Lan,Jiwan Ge,Jinfang Yu,Sisi Shan,Huan Zhou,Shilong Fan,Qi Zhang,Xuanling Shi,Qisheng Wang,Linqi Zhang,Xinquan Wang +10 more
TLDR
High-resolution crystal structures of the receptor-binding domain of the spike protein of SARS-CoV-2 and SARS -CoV in complex with ACE2 provide insights into the binding mode of these coronaviruses and highlight essential ACE2-interacting residues.Abstract:
A new and highly pathogenic coronavirus (severe acute respiratory syndrome coronavirus-2, SARS-CoV-2) caused an outbreak in Wuhan city, Hubei province, China, starting from December 2019 that quickly spread nationwide and to other countries around the world1–3. Here, to better understand the initial step of infection at an atomic level, we determined the crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 bound to the cell receptor ACE2. The overall ACE2-binding mode of the SARS-CoV-2 RBD is nearly identical to that of the SARS-CoV RBD, which also uses ACE2 as the cell receptor4. Structural analysis identified residues in the SARS-CoV-2 RBD that are essential for ACE2 binding, the majority of which either are highly conserved or share similar side chain properties with those in the SARS-CoV RBD. Such similarity in structure and sequence strongly indicate convergent evolution between the SARS-CoV-2 and SARS-CoV RBDs for improved binding to ACE2, although SARS-CoV-2 does not cluster within SARS and SARS-related coronaviruses1–3,5. The epitopes of two SARS-CoV antibodies that target the RBD are also analysed for binding to the SARS-CoV-2 RBD, providing insights into the future identification of cross-reactive antibodies. High-resolution crystal structures of the receptor-binding domain of the spike protein of SARS-CoV-2 and SARS-CoV in complex with ACE2 provide insights into the binding mode of these coronaviruses and highlight essential ACE2-interacting residues.read more
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Comparison of Severe Acute Respiratory Syndrome Coronavirus 2 Spike Protein Binding to ACE2 Receptors from Human, Pets, Farm Animals, and Putative Intermediate Hosts.
Xiaofeng Zhai,Jiumeng Sun,Ziqing Yan,Jie Zhang,Jin Zhao,Zongzheng Zhao,Qi Gao,Wan Ting He,Michael Veit,Shuo Su +9 more
TL;DR: X-ray structures of human ACE2 bound to the receptor-binding domain (RBD) of the spike protein (S) from SARS-CoV-2 are used to predict its binding to ACE2 proteins from different animals, including pets, farm animals, and putative intermediate hosts of Sars-Cov-2, and it is found that ACE2 from species known to support SATS infection tolerate many amino acid changes, indicating that the species barrier might be low.
Journal ArticleDOI
Mutations on RBD of SARS-CoV-2 Omicron variant result in stronger binding to human ACE2 receptor
Katrin von Kap-herr,Junwei Ma +1 more
TL;DR: In this article , the complex structure of the human ACE2 protein and the receptor binding domain (RBD) of Omicron Spike protein (S-protein) was modelled and atomistic molecular dynamics simulations were conducted to study the binding interactions.
Journal ArticleDOI
Functional and genetic analysis of viral receptor ACE2 orthologs reveals a broad potential host range of SARS-CoV-2.
Yinghui Liu,Gaowei Hu,Yuyan Wang,Wenlin Ren,Xiaomin Zhao,Fansen Ji,Yunkai Zhu,Fei Feng,Mingli Gong,Xiaohui Ju,Yuanfei Zhu,Xia Cai,Jun Lan,Jianying Guo,Min Xie,Lin Dong,Zihui Zhu,Jie Na,Jianping Wu,Xun Lan,Youhua Xie,Xinquan Wang,Zhenghong Yuan,Rong Zhang,Qiang Ding +24 more
TL;DR: In this article, the ability of angiotensin-converting enzyme 2 (ACE2) from diverse species to support SARS-CoV-2 entry to humans was characterized.
Journal ArticleDOI
Structure-guided covalent stabilization of coronavirus spike glycoprotein trimers in the closed conformation.
TL;DR: The design of a construct corresponding to the prefusion SARS-CoV-2 S ectodomain trimer is reported, covalently stabilized by a disulfide bond in the closed conformation, and might become an important tool for structural biology, serology, vaccine design and immunology studies.
Journal ArticleDOI
Liquid-liquid phase separation in human health and diseases.
Bin Wang,Bin Wang,Zhang Lei,Tong Dai,Ziran Qin,Ziran Qin,Huasong Lu,Long Zhang,Fangfang Zhou +8 more
TL;DR: A review of liquid-liquid phase separation (LLPS) in eukaryotic cells can be found in this paper, where the authors describe the current understanding of LLPS and summarize its physiological functions.
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