气候变化领域集成服务门户(CCPortal): Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2

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DOI	10.1126/science.abb2762
	Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2
	Yan R.; Zhang Y.; Li Y.; Xia L.; Guo Y.; Zhou Q.
发表日期	2020
ISSN	0036-8075
起始页码	1444
结束页码	1448
卷号	367 期号:6485
英文摘要	Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for severe acute respiratory syndrome–coronavirus (SARS-CoV) and the new coronavirus (SARS-CoV-2) that is causing the serious coronavirus disease 2019 (COVID-19) epidemic. Here, we present cryo–electron microscopy structures of full-length human ACE2 in the presence of the neutral amino acid transporter B0AT1 with or without the receptor binding domain (RBD) of the surface spike glycoprotein (S protein) of SARS-CoV-2, both at an overall resolution of 2.9 angstroms, with a local resolution of 3.5 angstroms at the ACE2-RBD interface. The ACE2-B0AT1 complex is assembled as a dimer of heterodimers, with the collectrin-like domain of ACE2 mediating homodimerization. The RBD is recognized by the extracellular peptidase domain of ACE2 mainly through polar residues. These findings provide important insights into the molecular basis for coronavirus recognition and infection. © 2020 American Association for the Advancement of Science. All rights reserved.
关键词	angiotensin converting enzyme 2 coronavirus spike glycoprotein heterodimer homodimer amino acid transporter angiotensin converting enzyme 2 dipeptidyl carboxypeptidase protein binding SLC6A19 protein, human spike protein, SARS-CoV-2 virus receptor enzyme gene gene expression protein ultrastructure virus Article binding site complex formation controlled study coronavirus disease 2019 cryoelectron microscopy dimerization embryo enzyme structure human human cell nonhuman priority journal protein domain SARS-related coronavirus Severe acute respiratory syndrome coronavirus 2 amino acid sequence Betacoronavirus Coronavirus infection molecular model pandemic protein multimerization SARS coronavirus sequence alignment ultrastructure virus pneumonia Coronavirus SARS coronavirus Amino Acid Sequence Amino Acid Transport Systems, Neutral Betacoronavirus Coronavirus Infections Cryoelectron Microscopy Humans Models, Molecular Pandemics Peptidyl-Dipeptidase A Pneumonia, Viral Protein Binding Protein Domains Protein Multimerization Receptors, Virus SARS Virus Sequence Alignment Spike Glycoprotein, Coronavirus
语种	英语
来源机构	Science
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/133606
推荐引用方式 GB/T 7714	Yan R.,Zhang Y.,Li Y.,et al. Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2[J]. Science,2020,367(6485).
APA	Yan R.,Zhang Y.,Li Y.,Xia L.,Guo Y.,&Zhou Q..(2020).Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2.,367(6485).
MLA	Yan R.,et al."Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2".367.6485(2020).