期刊
SCIENCE
卷 309, 期 5742, 页码 1864-1868出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1116480
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资金
- NCI NIH HHS [CA13202] Funding Source: Medline
- NIAID NIH HHS [AI061601] Funding Source: Medline
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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