Structure of SARS coronavirus spike receptor-binding domain complexed with receptor
Identifieur interne : 004D57 ( Main/Exploration ); précédent : 004D56; suivant : 004D58Structure 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 :
- Science : (Washington, D.C.) [ 0036-8075 ] ; 2005.
Descripteurs français
- Pascal (Inist)
English descriptors
- KwdEn :
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.
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream PascalFrancis, to step Corpus: 000588
- to stream PascalFrancis, to step Curation: 000402
- to stream PascalFrancis, to step Checkpoint: 000566
- to stream Main, to step Merge: 005086
- to stream Main, to step Curation: 004D57
Le document en format XML
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<front><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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<region><li>Massachusetts</li>
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<tree><country name="États-Unis"><region name="Massachusetts"><name sortKey="Fang Li" sort="Fang Li" uniqKey="Fang Li" last="Fang Li">FANG LI</name>
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<name sortKey="Farzan, Michael" sort="Farzan, Michael" uniqKey="Farzan M" first="Michael" last="Farzan">Michael Farzan</name>
<name sortKey="Harrison, Stephen C" sort="Harrison, Stephen C" uniqKey="Harrison S" first="Stephen C." last="Harrison">Stephen C. Harrison</name>
<name sortKey="Harrison, Stephen C" sort="Harrison, Stephen C" uniqKey="Harrison S" first="Stephen C." last="Harrison">Stephen C. Harrison</name>
<name sortKey="Wenhui Li" sort="Wenhui Li" uniqKey="Wenhui Li" last="Wenhui Li">WENHUI LI</name>
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