Structural biology: Structure of SARS coronavirus spike receptor-binding domain complexed with receptor

Fang Li, Wenhui Li, Michael Farzan, Stephen C. Harrison

Research output: Contribution to journalArticlepeer-review

750 Scopus citations

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 UBD bound with the peptidass 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.

Original languageEnglish (US)
Pages (from-to)1864-1868
Number of pages5
JournalScience
Volume309
Issue number5742
DOIs
StatePublished - Sep 16 2005

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