Structure of SARS coronavirus spike receptor-binding domain complexed with receptor
- PMID: 16166518
- DOI: 10.1126/science.1116480
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.
Comment in
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Structural biology. Adaptation of SARS coronavirus to humans.Science. 2005 Sep 16;309(5742):1822-3. doi: 10.1126/science.1118817. Science. 2005. PMID: 16166506 No abstract available.
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