The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Crystal structure of NL63 respiratory coronavirus receptor-binding domain complexed with its human receptor
Open accessAbstract
NL63 coronavirus (NL63-CoV), a prevalent human respiratory virus, is the only group I coronavirus known to use angiotensin-converting enzyme 2 (ACE2) as its receptor. Incidentally, ACE2 is also used by group II SARS coronavirus (SARS-CoV). We investigated how different groups of coronaviruses recognize the same receptor, whereas homologous group I coronaviruses recognize different receptors. We determined the crystal structure of NL63-CoV spike protein receptor-binding domain (RBD) complexed with human ACE2. NL63-CoV RBD has a novel β-sandwich core structure consisting of 2 layers of β-sheets, presenting 3 discontinuous receptor-binding motifs (RBMs) to bind ACE2. NL63-CoV and SARS-CoV have no structural homology in RBD cores or RBMs; yet the 2 viruses recognize common ACE2 regions, largely because of a “virus-binding hotspot” on ACE2. Among group I coronaviruses, RBD cores are conserved but RBMs are variable, explaining how these viruses recognize different receptors. These results provide a structural basis for understanding viral evolution and virus–receptor interactions.
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Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus
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Self-citationIdentification of a new human coronavirus
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Self-citationHuman aminopeptidase N is a receptor for human coronavirus 229E
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Cited by
Structure, function and antigenicity of the SARS-CoV-2 spike glycoprotein
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Self-citationStructural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2
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“The complex structures of hCoV-NL63 CTD and SARS-RBD bound to hACE2 have been reported previously (Li et al., 2005; Wu et al., 2009).”
Structure, Function, and Evolution of Coronavirus Spike Proteins
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Self-citationA serological assay to detect SARS-CoV-2 seroconversion in humans
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Metadata
- Authors
- Wu, K., Li, W., Peng, G., & Li, F.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2009-11-24
- Volume
- 106
- Issue
- 47
- Pages
- 19970-19974
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2143901293
- Cited by
- 355
- References
- 30
- FWCI
- 4.61
- Type
- journal article
- Language
- en
- Open access
- bronze
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