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.
Supporting text
Virus
Host
Location
Amino Acid Sequence
128
Amino Acid Substitution
82
Angiotensin-Converting Enzyme 2
178
Animals
1981
Antibodies, Viral
216
Binding Sites
90
Carboxypeptidases
6
Cell Line
162
Crystallography, X-Ray
32
Disease Outbreaks
174
Epitopes
17
Glycosylation
22
Humans
1455
Hydrophobic and Hydrophilic Interactions
2
Membrane Glycoproteins
26
Models, Molecular
99
Molecular Sequence Data
160
Mutation
211
Peptidyl-Dipeptidase A
58
Protein Conformation
44
Protein Structure, Tertiary
29
Receptors, Virus
208
Severe Acute Respiratory Syndrome
22
Severe acute respiratory syndrome-related coronavirus
79
