Structure of SARS Coronavirus Spike Receptor-Binding Domain Complexed with Receptor
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- Fang Li
- Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School and Laboratory of Molecular Medicine, 320 Longwood Avenue, Boston, MA 02115, USA.
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- Wenhui Li
- Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School and Laboratory of Molecular Medicine, 320 Longwood Avenue, Boston, MA 02115, USA.
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- Michael Farzan
- Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School and Laboratory of Molecular Medicine, 320 Longwood Avenue, Boston, MA 02115, USA.
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- Stephen C. Harrison
- Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School and Laboratory of Molecular Medicine, 320 Longwood Avenue, Boston, MA 02115, USA.
説明
<jats:p>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.</jats:p>
収録刊行物
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- Science
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Science 309 (5742), 1864-1868, 2005-09-16
American Association for the Advancement of Science (AAAS)
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詳細情報 詳細情報について
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- CRID
- 1360574094023873152
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- ISSN
- 10959203
- 00368075
- http://id.crossref.org/issn/00368075
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- データソース種別
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- Crossref