Structure of SARS coronavirus spike receptor-binding domain complexed with receptor.

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.
Mesh Terms:
Amino Acid Sequence, Amino Acid Substitution, Animals, Antibodies, Viral, Binding Sites, Carboxypeptidases, Cell Line, Crystallography, X-Ray, Disease Outbreaks, Epitopes, Glycosylation, Humans, Hydrophobic and Hydrophilic Interactions, Membrane Glycoproteins, Models, Molecular, Molecular Sequence Data, Mutation, Peptidyl-Dipeptidase A, Protein Conformation, Protein Structure, Tertiary, Receptors, Virus, SARS Virus, Severe Acute Respiratory Syndrome, Species Specificity, Viral Envelope Proteins, Viral Vaccines, Viverridae
Science
Date: Sep. 16, 2005
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