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Structure of SARS Coronavirus Spike Receptor-Binding Domain Complexed with Receptor
Abstract
The spike protein (S) of SARS coronavirus (SARS-CoV) attaches the virus to its cellular receptor, angiotensin-converting enzyme 2 (ACE2). A defined receptor-binding domain (RBD) on S mediates this interaction. The crystal structure at 2.9 angstrom resolution of the RBD bound with the peptidase domain of human ACE2 shows that the RBD presents a gently concave surface, which cradles the N-terminal lobe of the peptidase. The atomic details at the interface between the two proteins clarify the importance of residue changes that facilitate efficient cross-species infection and human-to-human transmission. The structure of the RBD suggests ways to make truncated disulfide-stabilized RBD variants for use in the design of coronavirus vaccines.
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Metadata
- Authors
- Li, F., Li, W., Farzan, M., & Harrison, S. C.
- Venue
- Science
- Published
- 2005-09-16
- Volume
- 309
- Issue
- 5742
- Pages
- 1864-1868
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1982533785
- Cited by
- 2,031
- References
- 2
- FWCI
- 22.61
- Type
- journal article
- Language
- en
- Open access
- closed
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