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

Identifieur interne : 004D57 ( Main/Exploration ); précédent : 004D56; suivant : 004D58

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

Auteurs : FANG LI [États-Unis] ; WENHUI LI [États-Unis] ; Michael Farzan [États-Unis] ; Stephen C. Harrison [États-Unis]

Source :

RBID : Pascal:05-0468606

Descripteurs français

English descriptors

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.


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Le document en format XML

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<div type="abstract" xml:lang="en">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.</div>
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