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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.